Conformational changes in redox pairs of protein structures

Fan, Samuel W., George, Richard A., Haworth, Naomi L., Feng, Lina L., Liu, Jason Y. and Wouters, Merridee A. 2009, Conformational changes in redox pairs of protein structures, Protein Science, vol. 18, no. 8, pp. 1745-1765.

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Title Conformational changes in redox pairs of protein structures
Author(s) Fan, Samuel W.
George, Richard A.
Haworth, Naomi L.
Feng, Lina L.
Liu, Jason Y.
Wouters, Merridee A.
Journal name Protein Science
Volume number 18
Issue number 8
Start page 1745
End page 1765
Publisher Wiley - Blackwell Publishing
Place of publication Hoboken, N. J.
Publication date 2009-08
ISSN 0961-8368
1469-896X
Keyword(s) disulfide redox activity
thiol-based redox signaling
OxyR
oxidative stress
CLIC1
zinc signaling
disordered proteins
molten globule
Summary 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.
Language eng
Field of Research 060199 Biochemistry and Cell Biology not elsewhere classified
Socio Economic Objective 970106 Expanding Knowledge in the Biological Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2009, Wiley - Blackwell Publishing
Persistent URL http://hdl.handle.net/10536/DRO/DU:30040264

Document type: Journal Article
Collection: School of Life and Environmental Sciences
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