RESUMEN
Through an expansive international effort that involved data collection on 12 small-angle X-ray scattering (SAXS) and four small-angle neutron scattering (SANS) instruments, 171 SAXS and 76 SANS measurements for five proteins (ribonuclease A, lysozyme, xylanase, urate oxidase and xylose isomerase) were acquired. From these data, the solvent-subtracted protein scattering profiles were shown to be reproducible, with the caveat that an additive constant adjustment was required to account for small errors in solvent subtraction. Further, the major features of the obtained consensus SAXS data over the q measurement range 0-1â Å-1 are consistent with theoretical prediction. The inherently lower statistical precision for SANS limited the reliably measured q-range to <0.5â Å-1, but within the limits of experimental uncertainties the major features of the consensus SANS data were also consistent with prediction for all five proteins measured in H2O and in D2O. Thus, a foundation set of consensus SAS profiles has been obtained for benchmarking scattering-profile prediction from atomic coordinates. Additionally, two sets of SAXS data measured at different facilities to q > 2.2â Å-1 showed good mutual agreement, affirming that this region has interpretable features for structural modelling. SAS measurements with inline size-exclusion chromatography (SEC) proved to be generally superior for eliminating sample heterogeneity, but with unavoidable sample dilution during column elution, while batch SAS data collected at higher concentrations and for longer times provided superior statistical precision. Careful merging of data measured using inline SEC and batch modes, or low- and high-concentration data from batch measurements, was successful in eliminating small amounts of aggregate or interparticle interference from the scattering while providing improved statistical precision overall for the benchmarking data set.
Asunto(s)
Benchmarking , Proteínas , Dispersión del Ángulo Pequeño , Difracción de Rayos X , Consenso , Reproducibilidad de los Resultados , Proteínas/química , SolventesRESUMEN
Cyclic peptide library screening technologies show immense promise for identifying drug leads and chemical probes for challenging targets. However, the structural and functional diversity encoded within such libraries is largely undefined. We have systematically profiled the affinity, selectivity, and structural features of library-derived cyclic peptides selected to recognize three closely related targets: the acetyllysine-binding bromodomain proteins BRD2, -3, and -4. We report affinities as low as 100 pM and specificities of up to 106-fold. Crystal structures of 13 peptide-bromodomain complexes reveal remarkable diversity in both structure and binding mode, including both α-helical and ß-sheet structures as well as bivalent binding modes. The peptides can also exhibit a high degree of structural preorganization. Our data demonstrate the enormous potential within these libraries to provide diverse binding modes against a single target, which underpins their capacity to yield highly potent and selective ligands.
Asunto(s)
Biblioteca de Péptidos , Péptidos Cíclicos , Sitios de Unión , Descubrimiento de Drogas , Humanos , Péptidos Cíclicos/química , Péptidos Cíclicos/metabolismo , Unión Proteica , Dominios Proteicos , Factores de Transcripción/química , Factores de Transcripción/metabolismoRESUMEN
Commensal bacteria serve as an important line of defense against colonisation by opportunisitic pathogens, but the underlying molecular mechanisms remain poorly explored. Here, we show that strains of a commensal bacterium, Haemophilus haemolyticus, make hemophilin, a heme-binding protein that inhibits growth of the opportunistic pathogen, non-typeable Haemophilus influenzae (NTHi) in culture. We purified the NTHi-inhibitory protein from H. haemolyticus and identified the hemophilin gene using proteomics and a gene knockout. An x-ray crystal structure of recombinant hemophilin shows that the protein does not belong to any of the known heme-binding protein folds, suggesting that it evolved independently. Biochemical characterisation shows that heme can be captured in the ferrous or ferric state, and with a variety of small heme-ligands bound, suggesting that hemophilin could function under a range of physiological conditions. Hemophilin knockout bacteria show a limited capacity to utilise free heme for growth. Our data suggest that hemophilin is a hemophore and that inhibition of NTHi occurs by heme starvation, raising the possibility that competition from hemophilin-producing H. haemolyticus could antagonise NTHi colonisation in the respiratory tract.
Asunto(s)
Haemophilus influenzae/efectos de los fármacos , Haemophilus/metabolismo , Proteínas de Unión al Hemo , Proteínas Bacterianas/química , Proteínas Bacterianas/aislamiento & purificación , Proteínas Bacterianas/farmacología , Infecciones por Haemophilus/microbiología , Infecciones por Haemophilus/prevención & control , Haemophilus influenzae/crecimiento & desarrollo , Hemo/metabolismo , Proteínas de Unión al Hemo/química , Proteínas de Unión al Hemo/aislamiento & purificación , Proteínas de Unión al Hemo/farmacología , HumanosRESUMEN
Tandem beta zippers are modular complexes formed between repeated linear motifs and tandemly arrayed domains of partner proteins in which ß-strands form upon binding. Studies of such complexes, formed by LIM domain proteins and linear motifs in their intrinsically disordered partners, revealed spacer regions between the linear motifs that are relatively flexible but may affect the overall orientation of the binding modules. We demonstrate that mutation of a solvent exposed side chain in the spacer region of an LHX4-ISL2 complex has no significant effect on the structure of the complex, but decreases binding affinity, apparently by increasing flexibility of the linker.
Asunto(s)
ADN Intergénico/ultraestructura , Proteínas de Unión al ADN/ultraestructura , Proteínas con Homeodominio LIM/ultraestructura , Factores de Transcripción/ultraestructura , Secuencia de Aminoácidos , Animales , Sitios de Unión/genética , ADN Intergénico/química , ADN Intergénico/genética , Proteínas de Unión al ADN/química , Proteínas de Unión al ADN/genética , Proteínas con Homeodominio LIM/química , Proteínas con Homeodominio LIM/genética , Ratones , Modelos Moleculares , Complejos Multiproteicos/química , Complejos Multiproteicos/genética , Complejos Multiproteicos/ultraestructura , Mutación/genética , Unión Proteica/genética , Estructura Secundaria de Proteína , Estructura Terciaria de Proteína , Homología de Secuencia de Aminoácido , Factores de Transcripción/química , Factores de Transcripción/genéticaRESUMEN
Understanding published research results should be through one's own eyes and include the opportunity to work with raw diffraction data to check the various decisions made in the analyses by the original authors. Today, preserving raw diffraction data is technically and organizationally viable at a growing number of data archives, both centralized and distributed, which are empowered to register data sets and obtain a preservation descriptor, typically a 'digital object identifier'. This introduces an important role of preserving raw data, namely understanding where we fail in or could improve our analyses. Individual science area case studies in crystallography are provided.
RESUMEN
In 2012, preliminary guidelines were published addressing sample quality, data acquisition and reduction, presentation of scattering data and validation, and modelling for biomolecular small-angle scattering (SAS) experiments. Biomolecular SAS has since continued to grow and authors have increasingly adopted the preliminary guidelines. In parallel, integrative/hybrid determination of biomolecular structures is a rapidly growing field that is expanding the scope of structural biology. For SAS to contribute maximally to this field, it is essential to ensure open access to the information required for evaluation of the quality of SAS samples and data, as well as the validity of SAS-based structural models. To this end, the preliminary guidelines for data presentation in a publication are reviewed and updated, and the deposition of data and associated models in a public archive is recommended. These guidelines and recommendations have been prepared in consultation with the members of the International Union of Crystallography (IUCr) Small-Angle Scattering and Journals Commissions, the Worldwide Protein Data Bank (wwPDB) Small-Angle Scattering Validation Task Force and additional experts in the field.
Asunto(s)
ADN/química , Políticas Editoriales , Proteínas/química , ARN/química , Dispersión del Ángulo Pequeño , Difracción de Rayos X , Animales , Bases de Datos de Proteínas , Humanos , Modelos MolecularesRESUMEN
The nuclear magnetic resonance (NMR) structure of the tri-helix bundle (THB) of the m-domain plus C2 (ΔmC2) of myosin-binding protein C (MyBP-C) has revealed a highly flexible seven-residue linker between the structured THB and C2. Bioinformatics shows significant patterns of conservation across the THB-linker sequence, with the linker containing a strictly conserved serine in all MyBP-C isoforms. Clinically linked mutations further support the functional significance of the THB-linker region. NMR, small-angle X-ray scattering, and binding studies show the THB-linker plus the first ten residues of C2 undergo dramatic changes when ΔmC2 binds Ca2+-calmodulin, with the linker and C2 N-terminal residues contributing significantly to the affinity. Modeling of all available experimental data indicates that the THB tertiary structure must be disrupted to form the complex. These results are discussed in the context of the THB-linker and the N-terminal residues of C2 forming a polymorphic binding domain that could accommodate multiple binding partners in the dynamic sarcomere.
Asunto(s)
Calmodulina/metabolismo , Proteínas Portadoras/química , Proteínas Portadoras/genética , Serina/metabolismo , Secuencia de Aminoácidos , Sitios de Unión , Proteínas Portadoras/metabolismo , Secuencia Conservada , Humanos , Modelos Moleculares , Resonancia Magnética Nuclear Biomolecular , Unión Proteica , Dominios Proteicos , Estructura Secundaria de Proteína , Estructura Terciaria de Proteína , Dispersión del Ángulo PequeñoRESUMEN
The structural effects of three missense mutations clinically linked to hypertrophic cardiomyopathy (HCM) and located in the central domains of cardiac myosin-binding protein C (cMyBP-C) have been determined using small-angle scattering, infrared spectroscopy, and nuclear magnetic resonance spectroscopy. Bioinformatics and modeling were used to initially predict the expected structural impacts and assess the broader implications for function based on sequence conservation patterns. The experimental results generally affirm the predictions that two of the mutations (D745G, P873H) disrupt domain folding, while the third (R820Q) is likely to be entirely solvent exposed and thus more likely to have its impact through its interactions within the sarcomere. Each of the mutations is associated with distinct disease phenotypes, with respect to severity, stage of onset, and end phase. The results are discussed in terms of understanding key structural features of these domains essential for healthy function and the role they may play in disease development.
Asunto(s)
Cardiomiopatía Hipertrófica/genética , Proteínas Portadoras/química , Mutación , Fenotipo , Secuencia de Aminoácidos , Animales , Sitios de Unión , Proteínas Portadoras/genética , Proteínas Portadoras/metabolismo , Humanos , Ratones , Datos de Secuencia Molecular , Unión ProteicaRESUMEN
Interprotein electron transfer underpins the essential processes of life and relies on the formation of specific, yet transient protein-protein interactions. In biological systems, the detoxification of sulfite is catalyzed by the sulfite-oxidizing enzymes (SOEs), which interact with an electron acceptor for catalytic turnover. Here, we report the structural and functional analyses of the SOE SorT from Sinorhizobium meliloti and its cognate electron acceptor SorU. Kinetic and thermodynamic analyses of the SorT/SorU interaction show the complex is dynamic in solution, and that the proteins interact with Kd = 13.5 ± 0.8 µM. The crystal structures of the oxidized SorT and SorU, both in isolation and in complex, reveal the interface to be remarkably electrostatic, with an unusually large number of direct hydrogen bonding interactions. The assembly of the complex is accompanied by an adjustment in the structure of SorU, and conformational sampling provides a mechanism for dissociation of the SorT/SorU assembly.
Asunto(s)
Proteínas Bacterianas/metabolismo , Transporte de Electrón , Oxidorreductasas/metabolismo , Sinorhizobium meliloti/metabolismo , Sulfitos/metabolismo , Proteínas Bacterianas/química , Cristalografía por Rayos X , Cinética , Modelos Moleculares , Oxidación-Reducción , Oxidorreductasas/genética , Unión Proteica , Conformación Proteica , Sinorhizobium meliloti/química , TermodinámicaRESUMEN
Staphylococcus aureus is a common and serious cause of infection in humans. The bacterium expresses a cell-surface receptor that binds to, and strips haem from, human haemoglobin (Hb). The binding interface has previously been identified; however, the structural changes that promote haem release from haemoglobin were unknown. Here, the structure of the receptor-Hb complex is reported at 2.6 Å resolution, which reveals a conformational change in the α-globin F helix that disrupts the haem-pocket structure and alters the Hb quaternary interactions. These features suggest potential mechanisms by which the S. aureus Hb receptor induces haem release from Hb.
Asunto(s)
Antígenos Bacterianos/química , Hemoglobinas/química , Receptores de Superficie Celular/química , Staphylococcus aureus/química , Globinas alfa/química , Modelos Moleculares , Conformación ProteicaRESUMEN
Haloalkane dehalogenases (HLDs) catalyse the hydrolysis of haloalkanes to alcohols, offering a biological solution for toxic haloalkane industrial wastes. Hundreds of putative HLD genes have been identified in bacterial genomes, but relatively few enzymes have been characterised. We identified two novel HLDs in the genome of Mycobacterium rhodesiae strain JS60, an isolate from an organochlorine-contaminated site: DmrA and DmrB. Both recombinant enzymes were active against C2-C6 haloalkanes, with a preference for brominated linear substrates. However, DmrA had higher activity against a wider range of substrates. The kinetic parameters of DmrA with 4-bromobutyronitrile as a substrate were Km = 1.9 ± 0.2 mM, kcat = 3.1 ± 0.2 s(-1) . DmrB showed the highest activity against 1-bromohexane. DmrA is monomeric, whereas DmrB is tetrameric. We determined the crystal structure of selenomethionyl DmrA to 1.7 Å resolution. A spacious active site and alternate conformations of a methionine side-chain in the slot access tunnel may contribute to the broad substrate activity of DmrA. We show that M. rhodesiaeâ JS60 can utilise 1-iodopropane, 1-iodobutane and 1-bromobutane as sole carbon and energy sources. This ability appears to be conferred predominantly through DmrA, which shows significantly higher levels of upregulation in response to haloalkanes than DmrB.
Asunto(s)
Alcanos/metabolismo , Hidrocarburos Halogenados/metabolismo , Hidrolasas/metabolismo , Mycobacterium/enzimología , Mycobacterium/metabolismo , Carbono/metabolismo , Dominio Catalítico , Cristalografía por Rayos X , ADN Bacteriano/química , ADN Bacteriano/genética , Metabolismo Energético , Microbiología Ambiental , Hidrolasas/química , Hidrolasas/genética , Hidrolasas/aislamiento & purificación , Hidrólisis , Cinética , Datos de Secuencia Molecular , Mycobacterium/crecimiento & desarrollo , Mycobacterium/aislamiento & purificación , Conformación Proteica , Análisis de Secuencia de ADN , Especificidad por SustratoRESUMEN
The IUCr Diffraction Data Deposition Working Group is investigating the rationale and policies for routine deposition of diffraction images (and other primary experimental data sets). An information-management framework is described that should inform policy directions, and some of the technical and other issues that need to be addressed in an effort to achieve such a goal are analysed. In the near future, routine data deposition could be encouraged at one of the growing number of institutional repositories that accept data sets or at a generic data-publishing web repository service. To realise all of the potential benefits of depositing diffraction data, specialized archives would be preferable. Funding such an initiative will be challenging.
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Curaduría de Datos/métodos , Difracción de Rayos X/métodos , Cristalografía por Rayos X , Bases de Datos Factuales , Bases de Datos de Proteínas , Ensayos Analíticos de Alto Rendimiento , Procesamiento de Imagen Asistido por Computador , Internet , Sociedades Científicas , SincrotronesRESUMEN
Adult haemoglobin (Hb) is made up of two α and two ß subunits. Mutations that reduce expression of the α- or ß-globin genes lead to the conditions α- or ß-thalassaemia, respectively. Whilst both conditions are characterized by anaemia of variable severity, other details of their pathophysiology are different, in part owing to the greater stability of the ß chains that is conferred through ß self-association. In contrast, α subunits interact weakly, and in the absence of stabilizing quaternary interactions the α chain (α) is prone to haem loss and denaturation. The molecular contacts that confer weak self-association of α have not been determined previously. Here, the first structure of an α2 homodimer is reported in complex with one domain of the Hb receptor from Staphylococcus aureus. The α2 dimer interface has a highly unusual, approximately linear, arrangement of four His side chains within hydrogen-bonding distance of each other. Some interactions present in the α1ß1 dimer interface of native Hb are preserved in the α2 dimer. However, a marked asymmetry is observed in the α2 interface, suggesting that steric factors limit the number of stabilizing interactions that can form simultaneously across the interface.
Asunto(s)
Hemoglobinas/química , Staphylococcus aureus/metabolismo , Cristalización , Cristalografía por Rayos X , Dimerización , Hemoglobinas/metabolismo , Unión Proteica , Conformación ProteicaRESUMEN
Staphylococcus aureus causes life-threatening disease in humans. The S. aureus surface protein iron-regulated surface determinant H (IsdH) binds to mammalian hemoglobin (Hb) and extracts heme as a source of iron, which is an essential nutrient for the bacteria. However, the process of heme transfer from Hb is poorly understood. We have determined the structure of IsdH bound to human Hb by x-ray crystallography at 4.2 Å resolution, revealing the structural basis for heme transfer. One IsdH molecule is bound to each α and ß Hb subunit, suggesting that the receptor acquires iron from both chains by a similar mechanism. Remarkably, two near iron transporter (NEAT) domains in IsdH perform very different functions. An N-terminal NEAT domain binds α/ß globin through a site distant from the globin heme pocket and, via an intervening structural domain, positions the C-terminal heme-binding NEAT domain perfectly for heme transfer. These data, together with a 2.3 Å resolution crystal structure of the isolated N-terminal domain bound to Hb and small-angle x-ray scattering of free IsdH, reveal how multiple domains of IsdH cooperate to strip heme from Hb. Many bacterial pathogens obtain iron from human hemoglobin using proteins that contain multiple NEAT domains and other domains whose functions are poorly understood. Our results suggest that, rather than acting as isolated units, NEAT domains may be integrated into higher order architectures that employ multiple interaction interfaces to efficiently extract heme from host proteins.
Asunto(s)
Antígenos Bacterianos/química , Hemo/química , Hemoglobinas/química , Hierro/metabolismo , Receptores de Superficie Celular/química , Infecciones Estafilocócicas/metabolismo , Staphylococcus aureus/metabolismo , Cristalografía por Rayos X , Humanos , Estructura Secundaria de Proteína , Estructura Terciaria de Proteína , Infecciones Estafilocócicas/sangreRESUMEN
Islet 1 (Isl1) is a transcription factor of the LIM-homeodomain (LIM-HD) protein family and is essential for many developmental processes. LIM-HD proteins all contain two protein-interacting LIM domains, a DNA-binding homeodomain (HD), and a C-terminal region. In Isl1, the C-terminal region also contains the LIM homeobox 3 (Lhx3)-binding domain (LBD), which interacts with the LIM domains of Lhx3. The LIM domains of Isl1 have been implicated in inhibition of DNA binding potentially through an intramolecular interaction with or close to the HD. Here we investigate the LBD as a candidate intramolecular interaction domain. Competitive yeast-two hybrid experiments indicate that the LIM domains and LBD from Isl1 can interact with apparently low affinity, consistent with no detection of an intermolecular interaction in the same system. Nuclear magnetic resonance studies show that the interaction is specific, whereas substitution of the LBD with peptides of the same amino acid composition but different sequence is not specific. We solved the crystal structure of a similar but higher affinity complex between the LIM domains of Isl1 and the LIM interaction domain from the LIM-HD cofactor protein LIM domain-binding protein 1 (Ldb1) and used these coordinates to generate a homology model of the intramolecular interaction that indicates poorer complementarity for the weak intramolecular interaction. The intramolecular interaction in Isl1 may provide protection against aggregation, minimize unproductive DNA binding, and facilitate cofactor exchange within the cell.
Asunto(s)
Proteínas con Homeodominio LIM/química , Proteínas con Homeodominio LIM/metabolismo , Estructura Terciaria de Proteína , Factores de Transcripción/química , Factores de Transcripción/metabolismo , Secuencia de Aminoácidos , Animales , Sitios de Unión/genética , Cristalografía por Rayos X , Proteínas con Homeodominio LIM/genética , Ratones , Modelos Moleculares , Datos de Secuencia Molecular , Mutación , Unión Proteica , Saccharomyces cerevisiae/genética , Factores de Transcripción/genética , Técnicas del Sistema de Dos HíbridosRESUMEN
Classical zinc fingers (ZFs) are one of the most abundant and best characterized DNA-binding domains. Typically, tandem arrays of three or more ZFs bind DNA target sequences with high affinity and specificity, and the mode of DNA recognition is sufficiently well understood that tailor-made ZF-based DNA-binding proteins can be engineered. We have shown previously that a two-zinc finger unit found in the transcriptional coregulator ZNF217 recognizes DNA but with an affinity and specificity that is lower than other ZF arrays. To investigate the basis for these differences, we determined the structure of a ZNF217-DNA complex. We show that although the overall position of the ZFs on the DNA closely resembles that observed for other ZFs, the side-chain interaction pattern differs substantially from the canonical model. The structure also reveals the presence of two methyl-π interactions, each featuring a tyrosine contacting a thymine methyl group. To our knowledge, interactions of this type have not previously been described in classical ZF-DNA complexes. Finally, we investigated the sequence specificity of this two-ZF unit and discuss how ZNF217 might discriminate its target DNA sites in the cell.
Asunto(s)
ADN/química , Modelos Moleculares , Proteínas de Neoplasias/química , Transactivadores/química , Cristalografía por Rayos X , ADN/metabolismo , Humanos , Proteínas de Neoplasias/metabolismo , Relación Estructura-Actividad , Transactivadores/metabolismo , Dedos de ZincRESUMEN
A stable intramolecular complex comprising the LIM domains of the LIM-homeodomain protein Isl1 tethered to a peptide region of Ldb1 has been engineered, purified and crystallized. The orthorhombic crystals belonged to space group P222(1), with unit-cell parameters a=57.2, b=56.7, c=179.8â Å, and diffracted to 3.10â Å resolution.
Asunto(s)
Proteínas de Unión al ADN/química , Proteínas con Dominio LIM/química , Proteínas con Homeodominio LIM/química , Factores de Transcripción/química , Animales , Cristalización , Cristalografía por Rayos X , Ratones , Complejos Multiproteicos/química , Estructura Terciaria de Proteína , Zinc/químicaRESUMEN
The N-terminal modules of cardiac myosin-binding protein C (cMyBP-C) play a regulatory role in mediating interactions between myosin and actin during heart muscle contraction. The so-called "motif," located between the second and third immunoglobulin modules of the cardiac isoform, is believed to modulate contractility via an "on-off" phosphorylation-dependent tether to myosin ΔS2. Here we report a novel Ca(2+)-dependent interaction between the motif and calmodulin (CaM) based on the results of a combined fluorescence, NMR, and light and x-ray scattering study. We show that constructs of cMyBP-C containing the motif bind to Ca(2+)/CaM with a moderate affinity (K(D) â¼10 µM), which is similar to the affinity previously determined for myosin ΔS2. However, unlike the interaction with myosin ΔS2, the Ca(2+)/CaM interaction is unaffected by substitution with a triphosphorylated motif mimic. Further, Ca(2+)/CaM interacts with the highly conserved residues (Glu(319)-Lys(341)) toward the C-terminal end of the motif. Consistent with the Ca(2+) dependence, the binding of CaM to the motif is mediated via the hydrophobic clefts within the N- and C-lobes that are known to become more exposed upon Ca(2+) binding. Overall, Ca(2+)/CaM engages with the motif in an extended clamp configuration as opposed to the collapsed binding mode often observed in other CaM-protein interactions. Our results suggest that CaM may act as a structural conduit that links cMyBP-C with Ca(2+) signaling pathways to help coordinate phosphorylation events and synchronize the multiple interactions between cMyBP-C, myosin, and actin during the heart muscle contraction.
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Calcio/química , Calmodulina/química , Proteínas Portadoras/química , Actinas/química , Actinas/genética , Actinas/metabolismo , Secuencias de Aminoácidos , Calcio/metabolismo , Calmodulina/genética , Calmodulina/metabolismo , Proteínas Portadoras/genética , Proteínas Portadoras/metabolismo , Humanos , Contracción Miocárdica/fisiología , Miocardio/química , Miocardio/metabolismo , Miosinas/química , Miosinas/genética , Miosinas/metabolismo , Resonancia Magnética Nuclear Biomolecular , Fosforilación/fisiología , Unión Proteica/fisiología , Estructura Terciaria de ProteínaRESUMEN
The X-ray crystal structure of oxidised pseudoazurin from the denitrifying plant symbiotic bacterium Sinorhizobium meliloti (SmPAz2) has been solved to a resolution of 2.0 Å. The pseudoazurin from Sinorhizobium sp. is unusual as it forms an operon with a sulfite dehydrogenase enzyme, rather than a Cu nitrite reductase. Examination of the structure reveals that the geometric parameters of the Type I Cu site in SmPAz2 correlate with observed features in the electronic spectrum of the protein. Comparison of the structure of SmPAz2 with those of pseudoazurins from five other bacterial species shows that the surface of SmPAz2 bears a conserved hydrophobic patch encircled by positively-charged residues, which may serve as a recognition site for its redox partners.
Asunto(s)
Azurina/química , Proteínas Bacterianas/química , Cobre/química , Sinorhizobium meliloti/química , Cristalografía por Rayos X , Estructura Terciaria de ProteínaRESUMEN
Small-angle scattering is becoming a mainstream technique for structural molecular biology. As such, it is important to establish guidelines for publication that will ensure that there is adequate reporting of the data and its treatment so that reviewers and readers can independently assess the quality of the data and the basis for any interpretations presented. This article presents a set of preliminary guidelines that emerged after consultation with the IUCr Commission on Small-Angle Scattering and other experts in the field and discusses the rationale for their application. At the 2011 Congress of the IUCr in Madrid, the Commission on Journals agreed to adopt these preliminary guidelines for the presentation of biomolecular structures from small-angle scattering data in IUCr publications. Here, these guidelines are outlined and the reasons for standardizing the way in which small-angle scattering data are presented.