Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1783, Issue 4, Pages 530-534Publisher
ELSEVIER
DOI: 10.1016/j.bbamcr.2008.02.009
Keywords
protein folding; disulfide bond formation; isomerization
Categories
Funding
- Howard Hughes Medical Institute Funding Source: Medline
- NIGMS NIH HHS [R01 GM057039, R01 GM064662, R01 GM064662-04, R01 GM064662-03, R01 GM057039-08, R01 GM057039-03, R01 GM057039-07, R01 GM064662-01A1, R01 GM057039-05, R01 GM057039-02, R01 GM057039-09, R01 GM057039-06, R01 GM057039-04, R01 GM064662-02] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM064662, R01GM057039] Funding Source: NIH RePORTER
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Proteins with multiple cysteine residues often require disulfide isomerization reactions before they attain their correct conformation. In prokaryotes this reaction is catalyzed mainly by DsbC, a protein that shares many similarities in structure and mechanism to the eukaryotic protein disulfide isomerase. This review discusses the current knowledge about disulfide isomerization in prokaryotes. (C) 2008 Elsevier B.V. All rights reserved.
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