4WZA

Asymmetric Nucleotide Binding in the Nitrogenase Complex

4WZA の概要

• エントリーDOI: 10.2210/pdb4wza/pdb
• 分子名称: Nitrogenase molybdenum-iron protein alpha chain, ADENOSINE-5'-DIPHOSPHATE, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, ... (12 entities in total)
• 機能のキーワード: nitrogenase, nucleotide binding, asymetry, complex, oxidoreductase
• 由来する生物種: Azotobacter vinelandii; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 353029.55

構造登録者

Tezcan, F.A.,Kaiser, J.T.,Howard, J.B.,Rees, D.C. (登録日: 2014-11-19, 公開日: 2014-12-31, 最終更新日: 2023-09-27)

主引用文献

Tezcan, F.A.,Kaiser, J.T.,Howard, J.B.,Rees, D.C.
Structural evidence for asymmetrical nucleotide interactions in nitrogenase.
J.Am.Chem.Soc., 137:146-149, 2015

PubMed Abstract: The roles of ATP hydrolysis in electron-transfer (ET) reactions of the nitrogenase catalytic cycle remain obscure. Here, we present a new structure of a nitrogenase complex crystallized with MgADP and MgAMPPCP, an ATP analogue. In this structure the two nucleotides are bound asymmetrically by the Fe-protein subunits connected to the two different MoFe-protein subunits. This binding mode suggests that ATP hydrolysis and phosphate release may proceed by a stepwise mechanism. Through the associated Fe-protein conformational changes, a stepwise mechanism is anticipated to prolong the lifetime of the Fe-protein-MoFe-protein complex and, in turn, could orchestrate the sequence of intracomplex ET required for substrate reduction.

PubMed: 25522159
DOI: 10.1021/ja511945e

実験手法

X-RAY DIFFRACTION (1.8995 Å)