Assuntos
Histiocitose/diagnóstico , Pólipos/diagnóstico , Gastropatias/diagnóstico , Proliferação de Células , Cristalização , Feminino , Gastrite/diagnóstico , Gastrite/microbiologia , Infecções por Helicobacter/complicações , Infecções por Helicobacter/diagnóstico , Helicobacter pylori/patogenicidade , Histiocitose/complicações , Histiocitose/patologia , Humanos , Pessoa de Meia-Idade , Plasmócitos , Pólipos/etiologia , Pólipos/patologia , Gastropatias/complicações , Gastropatias/patologiaRESUMO
The TB Structural Genomics Consortium is an organization devoted to encouraging, coordinating, and facilitating the determination and analysis of structures of proteins from Mycobacterium tuberculosis. The Consortium members hope to work together with other M. tuberculosis researchers to identify M. tuberculosis proteins for which structural information could provide important biological information, to analyze and interpret structures of M. tuberculosis proteins, and to work collaboratively to test ideas about M. tuberculosis protein function that are suggested by structure or related to structural information. This review describes the TB Structural Genomics Consortium and some of the proteins for which the Consortium is in the progress of determining three-dimensional structures.
Assuntos
Genômica/organização & administração , Mycobacterium tuberculosis/genética , Sequência de Aminoácidos , Proteínas de Bactérias/genética , Genoma Bacteriano , Humanos , Cooperação Internacional , Dados de Sequência Molecular , Mycobacterium tuberculosis/metabolismo , Conformação Proteica , Alinhamento de SequênciaRESUMO
Homologs of the Escherichia coli surE gene are present in many eubacteria and archaea. Despite the evolutionary conservation, little information is available on the structure and function of their gene products. We have determined the crystal structure of the SurE protein from Thermotoga maritima. The structure reveals the dimeric arrangement of the subunits and an active site around a bound metal ion. We also demonstrate that the SurE protein exhibits a divalent metal ion-dependent phosphatase activity that is inhibited by vanadate or tungstate. In the vanadate- and tungstate-complexed structures, the inhibitors bind adjacent to the divalent metal ion. Our structural and functional analyses identify the SurE proteins as a novel family of metal ion-dependent phosphatases.
Assuntos
Fosfatase Ácida , Proteínas de Bactérias/química , Proteínas de Bactérias/metabolismo , Proteínas de Escherichia coli , Fosfoproteínas Fosfatases/química , Fosfoproteínas Fosfatases/metabolismo , Thermotoga maritima/enzimologia , Sequência de Aminoácidos , Proteínas de Bactérias/antagonistas & inibidores , Proteínas de Bactérias/genética , Sítios de Ligação , Cátions Bivalentes/metabolismo , Cristalografia por Raios X , Metais/metabolismo , Modelos Moleculares , Dados de Sequência Molecular , Mutação/genética , Fosfoproteínas Fosfatases/antagonistas & inibidores , Fosfoproteínas Fosfatases/genética , Estrutura Secundária de Proteína , Estrutura Terciária de Proteína , Alinhamento de Sequência , Thermotoga maritima/genética , Compostos de Tungstênio/metabolismo , Compostos de Tungstênio/farmacologia , Vanadatos/metabolismo , Vanadatos/farmacologiaRESUMO
The surE protein from Thermotoga maritima is a 247-residue protein of unknown function. Its homologues are well conserved among both the eubacteria and the archaea. It has been overexpressed in soluble form in Escherichia coli. The protein has been crystallized at 296 K using 2-propanol as a precipitant. X-ray diffraction data have been collected to 1.9 A resolution using synchrotron radiation. The crystals belong to the trigonal space group P3(1)21 (or P3(2)21), with unit-cell parameters a = b = 115.96, c = 78.60 A, alpha = beta = 90, gamma = 120 degrees. The asymmetric unit contains two monomers of the surE protein, with a corresponding V(M) of 2.72 A(3) Da(-1) and a solvent content of 54.7%.
