Structural and functional characterization of Helicobacter pylori DsbG
Ji Young Yoon1, Jieun Kim, Sang Jae Lee
1Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul, Republic of Korea.
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.
Related Concept Videos
Gastritis II: Pathophysiology
Peptic Ulcer Disease III: Clinical Manifestations and Diagnostic Studies
Few clinical manifestations differentiate gastric ulcers from duodenal ulcers. Distinctions in the location, timing, and pain relief are crucial for healthcare providers in differentiating between gastric and duodenal ulcers during clinical assessments.
Peptic Ulcer
Bacterial Phylum Bacteroidota
Special Staining Techniques
Treating Helicobacter pylori in Peptic Ulcers: Antimicrobial Therapy


