6UG0

N2-bound Nitrogenase MoFe-protein from Azotobacter vinelandii

6UG0 の概要

• エントリーDOI: 10.2210/pdb6ug0/pdb
• 関連するPDBエントリー: 6VXT
• 分子名称: Nitrogenase molybdenum-iron protein alpha chain, GLYCEROL, TRIETHYLENE GLYCOL, ... (13 entities in total)
• 機能のキーワード: azotobacter vinelandii, mofe-protein, fe-protein, femo-cofactor, oxidized p-cluster, 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: 234901.75

構造登録者

Kang, W.,Hu, Y.,Ribbe, M.W. (登録日: 2019-09-25, 公開日: 2020-06-24, 最終更新日: 2023-10-11)

主引用文献

Kang, W.,Lee, C.C.,Jasniewski, A.J.,Ribbe, M.W.,Hu, Y.
Structural evidence for a dynamic metallocofactor during N2reduction by Mo-nitrogenase.
Science, 368:1381-1385, 2020

PubMed Abstract: The enzyme nitrogenase uses a suite of complex metallocofactors to reduce dinitrogen (N) to ammonia. Mechanistic details of this reaction remain sparse. We report a 1.83-angstrom crystal structure of the nitrogenase molybdenum-iron (MoFe) protein captured under physiological N turnover conditions. This structure reveals asymmetric displacements of the cofactor belt sulfurs (S2B or S3A and S5A) with distinct dinitrogen species in the two αβ dimers of the protein. The sulfur-displaced sites are distinct in the ability of protein ligands to donate protons to the bound dinitrogen species, as well as the elongation of either the Mo-O5 (carboxyl) or Mo-O7 (hydroxyl) distance that switches the Mo-homocitrate ligation from bidentate to monodentate. These results highlight the dynamic nature of the cofactor during catalysis and provide evidence for participation of all belt-sulfur sites in this process.

PubMed: 32554596
DOI: 10.1126/science.aaz6748

実験手法

X-RAY DIFFRACTION (1.83 Å)