AI Article Synopsis
- Proteins with numerous cysteine residues need disulfide isomerization to achieve their proper shape.
- In prokaryotes, this process is primarily facilitated by the protein DsbC, which has structural and functional similarities to the eukaryotic protein disulfide isomerase.
- The review focuses on the latest understanding of how disulfide isomerization occurs in prokaryotic organisms.
Article Abstract
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.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2391271 | PMC |
| http://dx.doi.org/10.1016/j.bbamcr.2008.02.009 | DOI Listing |
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