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Regulation of protein function: Crystal packing interfaces and conformational dimerization

Lookup NU author(s): Dr Susan Firbank, Dr Mark Banfield, Professor Christopher Dennison

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Abstract

The accepted view of interprotein electron transport involves molecules diffusing between donor and acceptor redox sites. An emerging alternative hypothesis is that efficient long-range electron transport can be achieved through proteins arranged in supramolecular assemblies. In this study, we have investigated the crystal packing interfaces in three crystal forms of plastocyanin, an integral component of the photosynthetic electron transport chain, and discuss their potential relevance to in vivo supramolecular assemblies. Symmetry-related protein chains within these crystals have Cu-Cu separations of <25 Å, a distance that readily supports electron transfer. In one structure, the plastocyanin molecule exists in two forms in which a backbone displacement coupled with side chain rearrangements enables the modulation of protein-protein interfaces. © 2008 American Chemical Society.


Publication metadata

Author(s): Crowley PB, Matias PM, Mi H, Firbank SJ, Banfield MJ, Dennison C

Publication type: Article

Publication status: Published

Journal: Biochemistry

Year: 2008

Volume: 47

Issue: 25

Pages: 6583-6589

ISSN (print): 0006-2960

ISSN (electronic): 1520-4995

Publisher: American Chemical Society

URL: http://dx.doi.org/10.1021/bi800125h

DOI: 10.1021/bi800125h


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