Structural and functional characterization of Helicobacter pylori DsbG.
FEBS Lett
; 585(24): 3862-7, 2011 Dec 15.
Article
em En
| MEDLINE
| ID: mdl-22062156
ABSTRACT
Dsb proteins play important roles in bacterial pathogenicity. To better understand the role of Dsb proteins in Helicobacter pylori, we have structurally and functionally characterized H. pylori DsbG (HP0231). The monomer consists of two domains connected by a helical linker. Two monomers associate to form a V-shaped dimer. The monomeric and dimeric structures of H. pylori DsbG show significant differences compared to Escherichia coli DsbG. Two polyethylene glycol molecules are bound in the cleft of the V-shaped dimer, suggesting a possible role as a chaperone. Furthermore, we show that H. pylori DsbG functions as a reductase against HP0518, a putative L,D-transpeptidase with a catalytic cysteine residue.
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1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oxirredutases
/
Helicobacter pylori
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2011
Tipo de documento:
Article