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Conformational changes in redox pairs of protein structures

journal contribution
posted on 2009-08-01, 00:00 authored by S Fan, R George, N Haworth, L Feng, J Liu, Merridee Wouters
Disulfides are conventionally viewed as structurally stabilizing elements in proteins but emerging evidence suggests two disulfide subproteomes exist. One group mediates the well known role of structural stabilization. A second redox-active group are best known for their catalytic functions but are increasingly being recognized for their roles in regulation of protein function. Redox-active disulfides are, by their very nature, more susceptible to reduction than structural disulfides; and conversely, the Cys pairs that form them are more susceptible to oxidation. In this study, we searched for potentially redox-active Cys Pairs by scanning the Protein Data Bank for structures of proteins in alternate redox states. The PDB contains over 1134 unique redox pairs of proteins, many of which exhibit conformational differences between alternate redox states. Several classes of structural changes were observed, proteins that exhibit: disulfide oxidation following expulsion of metals such as zinc; major reorganisation of the polypeptide backbone in association with disulfide redox-activity; order/disorder transitions; and changes in quaternary structure. Based on evidence gathered supporting disulfide redox activity, we propose disulfides present in alternate redox states are likely to have physiologically relevant redox activity.

History

Journal

Protein Science

Volume

18

Issue

8

Pagination

1745 - 1765

Publisher

Wiley - Blackwell Publishing

Location

Hoboken, N. J.

ISSN

0961-8368

eISSN

1469-896X

Language

eng

Publication classification

C1.1 Refereed article in a scholarly journal

Copyright notice

2009, Wiley - Blackwell Publishing