Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labeling

Export of protein into the periplasm of Escherichia coli via the general secretory system requires that the transported polypeptides be devoid of stably folded tertiary structure. Capture of the precursor polypeptides before they fold is achieved by the promiscuous binding to the chaperone SecB. Sec...

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Bibliographic Details
Main Authors: Crane, Jennine M., Suo, Yuying, Lilly, Angela A., Mao, Chunfeng, Hubbell, Wayne L., Randall, Linda L.
Format: Artigo
Language:Inglês
Published: 2006
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Article
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC2925277/
https://ncbi.nlm.nih.gov/pubmed/16962134
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2006.07.021
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