3TDG

Structural and functional characterization of Helicobacter pylori DsbG

3TDG の概要

• エントリーDOI: 10.2210/pdb3tdg/pdb
• 分子名称: Putative uncharacterized protein, GLYCEROL, FORMIC ACID, ... (5 entities in total)
• 機能のキーワード: thioredoxin fold, reductase, oxidoreductase
• 由来する生物種: Helicobacter pylori
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30991.73

構造登録者

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. (登録日: 2011-08-11, 公開日: 2011-11-09, 最終更新日: 2024-03-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.1 Å)