1D3W

Crystal structure of ferredoxin 1 d15e mutant from azotobacter vinelandii at 1.7 angstrom resolution.

1D3W の概要

• エントリーDOI: 10.2210/pdb1d3w/pdb
• 関連するPDBエントリー: 1BOT 1FDD 6FDR 7FDR
• 分子名称: FERREDOXIN 1, IRON/SULFUR CLUSTER, FE3-S4 CLUSTER, ... (4 entities in total)
• 機能のキーワード: beta sheet, protein monomer, iron-sulphur protein, ferredoxin, electron transport
• 由来する生物種: Azotobacter vinelandii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12720.99

構造登録者

Chen, K.,Hirst, J.,Camba, R.,Bonagura, C.A.,Stout, C.D.,Burges, B.K.,Armstrong, F.A. (登録日: 1999-10-01, 公開日: 1999-10-14, 最終更新日: 2024-02-07)

主引用文献

Chen, K.,Hirst, J.,Camba, R.,Bonagura, C.A.,Stout, C.D.,Burgess, B.K.,Armstrong, F.A.
Atomically defined mechanism for proton transfer to a buried redox centre in a protein.
Nature, 405:814-817, 2000

PubMed Abstract: The basis of the chemiosmotic theory is that energy from light or respiration is used to generate a trans-membrane proton gradient. This is largely achieved by membrane-spanning enzymes known as 'proton pumps. There is intense interest in experiments which reveal, at the molecular level, how protons are drawn through proteins. Here we report the mechanism, at atomic resolution, for a single long-range electron-coupled proton transfer. In Azotobacter vinelandii ferredoxin I, reduction of a buried iron-sulphur cluster draws in a solvent proton, whereas re-oxidation is 'gated' by proton release to the solvent. Studies of this 'proton-transferring module' by fast-scan protein film voltammetry, high-resolution crystallography, site-directed mutagenesis and molecular dynamics, reveal that proton transfer is exquisitely sensitive to the position and pK of a single amino acid. The proton is delivered through the protein matrix by rapid penetrative excursions of the side-chain carboxylate of a surface residue (Asp 15), whose pK shifts in response to the electrostatic charge on the iron-sulphur cluster. Our analysis defines the structural, dynamic and energetic requirements for proton courier groups in redox-driven proton-pumping enzymes.

PubMed: 10866206
DOI: 10.1038/35015610

実験手法

X-RAY DIFFRACTION (1.7 Å)