8RHO

[2Fe:2S] ferredoxin FeSII from Azotobacter vinelandii, reduced form

8RHO の概要

• エントリーDOI: 10.2210/pdb8rho/pdb
• 分子名称: Ferredoxin, FE2/S2 (INORGANIC) CLUSTER, 1,2-ETHANEDIOL, ... (6 entities in total)
• 機能のキーワード: [2fe:2s] ferredoxin fesii, metal binding protein
• 由来する生物種: Azotobacter vinelandii DJ
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27735.21

構造登録者

Franke, P.,Zhang, L.,Einsle, O. (登録日: 2023-12-15, 公開日: 2025-01-01, 最終更新日: 2025-02-05)

主引用文献

Franke, P.,Freiberger, S.,Zhang, L.,Einsle, O.
Conformational protection of molybdenum nitrogenase by Shethna protein II.
Nature, 637:998-1004, 2025

PubMed Abstract: The oxygen-sensitive molybdenum-dependent nitrogenase of Azotobacter vinelandii is protected from oxidative damage by a reversible 'switch-off' mechanism. It forms a complex with a small ferredoxin, FeSII (ref. ) or the 'Shethna protein II', which acts as an O sensor and associates with the two component proteins of nitrogenase when its [2Fe:2S] cluster becomes oxidized. Here we report the three-dimensional structure of the protective ternary complex of the catalytic subunit of Mo-nitrogenase, its cognate reductase and the FeSII protein, determined by single-particle cryo-electron microscopy. The dimeric FeSII protein associates with two copies of each component to assemble a 620 kDa core complex that then polymerizes into large, filamentous structures. This complex is catalytically inactive, but the enzyme components are quickly released and reactivated upon oxygen depletion. The first step in complex formation is the association of FeSII with the more O-sensitive Fe protein component of nitrogenase during sudden oxidative stress. The action of this small ferredoxin represents a straightforward means of protection from O that may be crucial for the maintenance of recombinant nitrogenase in food crops.

PubMed: 39779845
DOI: 10.1038/s41586-024-08355-3

実験手法

X-RAY DIFFRACTION (1.45 Å)