2JXM

Ensemble of twenty structures of the Prochlorothrix hollandica plastocyanin- cytochrome f complex

2JXM の概要

• エントリーDOI: 10.2210/pdb2jxm/pdb
• 関連するPDBエントリー: 1B3I 1CI3
• 分子名称: Plastocyanin, Cytochrome f, COPPER (II) ION, ... (4 entities in total)
• 機能のキーワード: copper, electron transport, metal-binding, transport
• 由来する生物種: Prochlorothrix hollandica; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37442.19

構造登録者

Hulsker, R.,Baranova, M.,Bullerjahn, G.,Ubbink, M. (登録日: 2007-11-22, 公開日: 2008-02-12, 最終更新日: 2024-05-29)

主引用文献

Hulsker, R.,Baranova, M.V.,Bullerjahn, G.S.,Ubbink, M.
Dynamics in the transient complex of plastocyanin-cytochrome f from Prochlorothrix hollandica.
J.Am.Chem.Soc., 130:1985-1991, 2008

PubMed Abstract: The nature of transient protein complexes can range from a highly dynamic ensemble of orientations to a single well-defined state. This represents variation in the equilibrium between the encounter and final, functional state. The transient complex between plastocyanin (Pc) and cytochrome f (cytf) of the cyanobacterium Prochlorothrix hollandica was characterized by NMR spectroscopy. Intermolecular pseudocontact shifts and chemical shift perturbations were used as restraints in docking calculations to determine the structure of the wild-type Pc-cytf complex. The orientation of Pc is similar to orientations found in Pc-cytf complexes from other sources. Electrostatics seems to play a modest role in complex formation. A large variability in the ensemble of lowest energy structures indicates a dynamic nature of the complex. Two unusual hydrophobic patch residues in Pc have been mutated to the residues found in other plastocyanins (Y12G/P14L). The binding constants are similar for the complexes of cytf with wild-type Pc and mutant Pc, but the chemical shift perturbations are smaller for the complex with mutant Pc. Docking calculations for the Y12G/P14L Pc-cytf complex did not produce a converged ensemble of structures. Simulations of the dynamics were performed using the observed averaged NMR parameters as input. The results indicate a surprisingly large amplitude of mobility of Y12G/P14L Pc within the complex. It is concluded that the double mutation shifts the complex further from the well-defined toward the encounter state.

PubMed: 18201089
DOI: 10.1021/ja077453p

実験手法

SOLUTION NMR