3CVC

Regulation of Protein Function: Crystal Packing Interfaces and Conformational Dimerization

3CVC の概要

• エントリーDOI: 10.2210/pdb3cvc/pdb
• 関連するPDBエントリー: 1baw 3cvb 3cvd
• 分子名称: Plastocyanin, COPPER (II) ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: cupredoxin, self assembly, copper, electron transport, metal-binding, transport
• 由来する生物種: Phormidium laminosum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11553.67

構造登録者

Crowley, P.B.,Matias, P.M.,Mi, H.,Firbank, S.J.,Banfield, M.J.,Dennison, C. (登録日: 2008-04-18, 公開日: 2008-07-08, 最終更新日: 2024-02-21)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.72 Å)