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Article

Crystal structure of the periplasmic disulfide-bond isomerase DsbC from Salmonella enterica serovar Typhimurium and the mechanistic implications.

Journal of structural biology - 1 Jul 2013

Jiao Li, Kim Jin-Sik, Song Woo-Seok, Yoon Bo-Young, Lee Kangseok, Ha Nam-Chul

Abstract excerpt

The disulfide-bond isomerase DsbC plays a crucial role in the folding of bacterial proteins in the periplasmic space. DsbC has a V-shaped dimeric structure with two domains, and Cys98 in the C-terminal domain attacks inappropriate disulfide bonds in substrate proteins due to its high nucleophilic activity. In this article, we present the crystal structure of DsbC from Salmonella enterica serovar Typhimurium. We...

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Identifiers

PMID: 23726983
DOI: 10.1016/j.jsb.2013.05.013

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

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