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Article

Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity.

The EMBO journal - 15 Apr 1994

Shevchik V E, Condemine G, Robert-Baudouy J

Abstract excerpt

We identified and characterized an Erwinia chrysanthemi gene able to complement an Escherichia coli dsbA mutation that prevents disulfide bond formation in periplasmic proteins. This gene, dsbC, codes for a 24 kDa periplasmic protein that contains a characteristic active site sequence of disulfide isomerases, Phe-X-X-X-X-Cys-X-X-Cys. Besides the active site, DsbC has no homology with DsbA, thioredoxin or...

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Identifiers

PMID: 8168497
DOI: 10.1002/j.1460-2075.1994.tb06470.x
PMCID: PMC395043

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Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity.PMID 8168497Read ↗

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