3CVD

Regulation of Protein Function: Crystal Packing Interfaces and Conformational Dimerization

Summary for 3CVD

• Entry DOI: 10.2210/pdb3cvd/pdb
• Related: 1baw 3cvb 3cvc
• Descriptor: Plastocyanin, COPPER (I) ION, ZINC ION, ... (4 entities in total)
• Functional Keywords: cupredoxin, self assemby, copper, electron transport, metal-binding, transport
• Biological source: Phormidium laminosum
• Total number of polymer chains: 3
• Total formula weight: 34849.72

Authors

Crowley, P.B.,Matias, P.M.,Mi, H.,Firbank, S.J.,Banfield, M.J.,Dennison, C. (deposition date: 2008-04-18, release date: 2008-07-08, Last modification date: 2024-02-21)

Primary citation

Crowley, P.B.,Matias, P.M.,Mi, H.,Firbank, S.J.,Banfield, M.J.,Dennison, C.
Regulation of protein function: crystal packing interfaces and conformational dimerization.
Biochemistry, 47:6583-6589, 2008

PubMed 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 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.

PubMed: 18479147
DOI: 10.1021/bi800125h

Experimental method

X-RAY DIFFRACTION (1.5 Å)