Structural highlights
Publication Abstract from PubMed
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.
Structural and functional characterization of Helicobacter pylori DsbG.,Yoon JY, Kim J, Lee SJ, Kim HS, Im HN, Yoon HJ, Kim KH, Kim SJ, Han BW, Suh SW FEBS Lett. 2011 Dec 15;585(24):3862-7. doi: 10.1016/j.febslet.2011.10.042. Epub, 2011 Nov 2. PMID:22062156[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yoon JY, Kim J, Lee SJ, Kim HS, Im HN, Yoon HJ, Kim KH, Kim SJ, Han BW, Suh SW. Structural and functional characterization of Helicobacter pylori DsbG. FEBS Lett. 2011 Dec 15;585(24):3862-7. doi: 10.1016/j.febslet.2011.10.042. Epub, 2011 Nov 2. PMID:22062156 doi:10.1016/j.febslet.2011.10.042
