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ERp57 Is a Multifunctional Thiol-Disulfide Oxidoreductase
The thiol-disulfide oxidoreductase ERp57 is a soluble protein of the endoplasmic reticulum and the closest known homologue of protein disulfide isomerase. The protein interacts with the two lectin chaperones calnexin and calreticulin and thereby promotes the oxidative folding of newly synthesized gl...
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Published in: | The Journal of biological chemistry 2004-04, Vol.279 (18), p.18277-18287 |
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Main Authors: | , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | The thiol-disulfide oxidoreductase ERp57 is a soluble protein of the endoplasmic reticulum and the closest known homologue
of protein disulfide isomerase. The protein interacts with the two lectin chaperones calnexin and calreticulin and thereby
promotes the oxidative folding of newly synthesized glycoproteins. Here we have characterized several fundamental structural
and functional properties of ERp57 in vitro , such as the domain organization, shape, redox potential, and the ability to catalyze different thiol-disulfide exchange
reactions. Like protein disulfide isomerase, we find ERp57 to be comprised of four structural domains. The protein has an
elongated shape of 3.4 ± 0.1 nm in diameter and 16.8 ± 0.5 nm in length. The two redox-active a and aⲠdomains were determined
to have redox potentials of â0.167 and â0.156 V, respectively. Furthermore, ERp57 was shown to efficiently catalyze disulfide
reduction, disulfide isomerization, and dithiol oxidation in substrate proteins. The implications of these findings for the
function of the protein in vivo are discussed. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1074/jbc.M314089200 |