4TKU

Reactivated Nitrogenase MoFe-protein from A. vinelandii

4TKU の概要

• エントリーDOI: 10.2210/pdb4tku/pdb
• 関連するPDBエントリー: 1M1N 3U7Q 4TKV
• 分子名称: Nitrogenase molybdenum-iron protein alpha chain, Nitrogenase molybdenum-iron protein beta chain, 3-HYDROXY-3-CARBOXY-ADIPIC ACID, ... (9 entities in total)
• 機能のキーワード: nitrogenase, femo-cofactor, inhibition, oxidoreductase
• 由来する生物種: Azotobacter vinelandii; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 233860.78

構造登録者

Spatzal, T.,Perez, K.,Einsle, O.,Howard, J.B.,Rees, D.C. (登録日: 2014-05-27, 公開日: 2014-10-01, 最終更新日: 2023-12-27)

主引用文献

Spatzal, T.,Perez, K.A.,Einsle, O.,Howard, J.B.,Rees, D.C.
Ligand binding to the FeMo-cofactor: structures of CO-bound and reactivated nitrogenase.
Science, 345:1620-1623, 2014

PubMed Abstract: The mechanism of nitrogenase remains enigmatic, with a major unresolved issue concerning how inhibitors and substrates bind to the active site. We report a crystal structure of carbon monoxide (CO)-inhibited nitrogenase molybdenum-iron (MoFe)-protein at 1.50 angstrom resolution, which reveals a CO molecule bridging Fe2 and Fe6 of the FeMo-cofactor. The μ2 binding geometry is achieved by replacing a belt-sulfur atom (S2B) and highlights the generation of a reactive iron species uncovered by the displacement of sulfur. The CO inhibition is fully reversible as established by regain of enzyme activity and reappearance of S2B in the 1.43 angstrom resolution structure of the reactivated enzyme. The substantial and reversible reorganization of the FeMo-cofactor accompanying CO binding was unanticipated and provides insights into a catalytically competent state of nitrogenase.

PubMed: 25258081
DOI: 10.1126/science.1256679

実験手法

X-RAY DIFFRACTION (1.43 Å)