3TDG

Structural and functional characterization of Helicobacter pylori DsbG

Summary for 3TDG

• Entry DOI: 10.2210/pdb3tdg/pdb
• Descriptor: Putative uncharacterized protein, GLYCEROL, FORMIC ACID, ... (5 entities in total)
• Functional Keywords: thioredoxin fold, reductase, oxidoreductase
• Biological source: Helicobacter pylori
• Total number of polymer chains: 1
• Total formula weight: 30991.73

Authors

Yoon, J.Y.,Kim, J.,Lee, S.J.,Kim, H.S.,Im, H.N.,Yoon, H.,Kim, K.H.,Kim, S.,Han, B.W.,Suh, S.W. (deposition date: 2011-08-11, release date: 2011-11-09, Last modification date: 2024-03-20)

Primary citation

Yoon, J.Y.,Kim, J.,Lee, S.J.,Kim, H.S.,Im, H.N.,Yoon, H.,Kim, K.H.,Kim, S.,Han, B.W.,Suh, S.W.
Structural and functional characterization of Helicobacter pylori DsbG
Febs Lett., 585:3862-3867, 2011

PubMed 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.

PubMed: 22062156
DOI: 10.1016/j.febslet.2011.10.042

Experimental method

X-RAY DIFFRACTION (2.1 Å)