Detalhe da pesquisa
1.
The structure of Mlc titration factor A (MtfA/YeeI) reveals a prototypical zinc metallopeptidase related to anthrax lethal factor.
J Bacteriol
; 194(11): 2987-99, 2012 Jun.
Artigo
em Inglês
| MEDLINE | ID: mdl-22467785
2.
Structural basis of murein peptide specificity of a gamma-D-glutamyl-l-diamino acid endopeptidase.
Structure
; 17(2): 303-13, 2009 Feb 13.
Artigo
em Inglês
| MEDLINE | ID: mdl-19217401
3.
Structural and functional characterizations of SsgB, a conserved activator of developmental cell division in morphologically complex actinomycetes.
J Biol Chem
; 284(37): 25268-79, 2009 Sep 11.
Artigo
em Inglês
| MEDLINE | ID: mdl-19567872
4.
Structure of the first representative of Pfam family PF09410 (DUF2006) reveals a structural signature of the calycin superfamily that suggests a role in lipid metabolism.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 10): 1153-9, 2010 Oct 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-20944205
5.
The structure of SSO2064, the first representative of Pfam family PF01796, reveals a novel two-domain zinc-ribbon OB-fold architecture with a potential acyl-CoA-binding role.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 10): 1160-6, 2010 Oct 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-20944206
6.
Structure of the first representative of Pfam family PF04016 (DUF364) reveals enolase and Rossmann-like folds that combine to form a unique active site with a possible role in heavy-metal chelation.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 10): 1167-73, 2010 Oct 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-20944207
7.
The structure of the first representative of Pfam family PF09836 reveals a two-domain organization and suggests involvement in transcriptional regulation.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 10): 1174-81, 2010 Oct 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-20944208
8.
Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 10): 1182-9, 2010 Oct 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-20944209
9.
The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45â Å resolution reveals a new fold (the ABATE domain) and suggests its possible role as a transcription regulator.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 10): 1198-204, 2010 Oct 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-20944211
10.
Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino-acid metabolism.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 10): 1205-10, 2010 Oct 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-20944212
11.
The structure of the first representative of Pfam family PF06475 reveals a new fold with possible involvement in glycolipid metabolism.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 10): 1211-7, 2010 Oct 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-20944213
12.
Structures of the first representatives of Pfam family PF06938 (DUF1285) reveal a new fold with repeated structural motifs and possible involvement in signal transduction.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 10): 1218-25, 2010 Oct 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-20944214
13.
Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5â Å resolution.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 10): 1230-6, 2010 Oct 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-20944216
14.
Structure of a putative NTP pyrophosphohydrolase: YP_001813558.1 from Exiguobacterium sibiricum 255-15.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 10): 1237-44, 2010 Oct 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-20944217
15.
Open and closed conformations of two SpoIIAA-like proteins (YP_749275.1 and YP_001095227.1) provide insights into membrane association and ligand binding.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 10): 1245-53, 2010 Oct 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-20944218
16.
The structure of KPN03535 (gi|152972051), a novel putative lipoprotein from Klebsiella pneumoniae, reveals an OB-fold.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 10): 1254-60, 2010 Oct 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-20944219
17.
The structure of BVU2987 from Bacteroides vulgatus reveals a superfamily of bacterial periplasmic proteins with possible inhibitory function.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 10): 1265-73, 2010 Oct 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-20944221
18.
Structure of BT_3984, a member of the SusD/RagB family of nutrient-binding molecules.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 10): 1274-80, 2010 Oct 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-20944222
19.
A conserved fold for fimbrial components revealed by the crystal structure of a putative fimbrial assembly protein (BT1062) from Bacteroides thetaiotaomicron at 2.2â Å resolution.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 10): 1281-6, 2010 Oct 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-20944223
20.
Structure of Bacteroides thetaiotaomicron BT2081 at 2.05â Å resolution: the first structural representative of a new protein family that may play a role in carbohydrate metabolism.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 10): 1287-96, 2010 Oct 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-20944224