Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
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 A, 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.
Regulation of Protein Function: Crystal Packing Interfaces and Conformational Dimerization.,Crowley PB, Matias PM, Mi H, Firbank SJ, Banfield MJ, Dennison C Biochemistry. 2008 May 15;. PMID:18479147[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Crowley PB, Matias PM, Mi H, Firbank SJ, Banfield MJ, Dennison C. Regulation of Protein Function: Crystal Packing Interfaces and Conformational Dimerization. Biochemistry. 2008 May 15;. PMID:18479147 doi:10.1021/bi800125h
