title: Structural and functional characterization of Helicobacter pylori DsbG.
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.
authors: Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul, Republic of Korea.
authors: Ji Young
authors: JY
authors: Yoon
authors: Jieun
authors: J
authors: Kim
authors: Sang Jae
authors: SJ
authors: Lee
authors: Hyoun Sook
authors: HS
authors: Kim
authors: Ha Na
authors: HN
authors: Im
authors: Hye-Jin
authors: HJ
authors: Yoon
authors: Kyoung Hoon
authors: KH
authors: Kim
authors: Soon-Jong
authors: SJ
authors: Kim
authors: Byung Woo
authors: BW
authors: Han
authors: Se Won
authors: SW
authors: Suh
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism; D020134:Catalytic Domain; D004926:Escherichia coli / Q000201:enzymology; D016480:Helicobacter pylori / Q000201:enzymology* / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D008958:Models, Molecular; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry* / Q000378:metabolism*; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary
chemical_list: D001426:Bacterial Proteins; C079503:DsbB protein, Bacteria; D008565:Membrane Proteins; D010088:Oxidoreductases