5BVH

CO-bound form of Selenium incorporated nitrogenase MoFe-protein (Av1-Se-CO) from A. vinelandii

5BVH の概要

• エントリーDOI: 10.2210/pdb5bvh/pdb
• 関連するPDBエントリー: 5BVG
• 分子名称: Nitrogenase molybdenum-iron protein alpha chain, FE (II) ION, Nitrogenase molybdenum-iron protein beta chain, ... (11 entities in total)
• 機能のキーワード: nitrogenase, femo-cofactor, se-incorporation, 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: 235773.08

構造登録者

Spatzal, T.,Perez, K.A.,Howard, J.B.,Rees, D.C. (登録日: 2015-06-05, 公開日: 2015-12-30, 最終更新日: 2024-10-30)

主引用文献

Spatzal, T.,Perez, K.A.,Howard, J.B.,Rees, D.C.
Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor.
Elife, 4:e11620-e11620, 2015

PubMed Abstract: Dinitrogen reduction in the biological nitrogen cycle is catalyzed by nitrogenase, a two-component metalloenzyme. Understanding of the transformation of the inert resting state of the active site FeMo-cofactor into an activated state capable of reducing dinitrogen remains elusive. Here we report the catalysis dependent, site-selective incorporation of selenium into the FeMo-cofactor from selenocyanate as a newly identified substrate and inhibitor. The 1.60 Å resolution structure reveals selenium occupying the S2B site of FeMo-cofactor in the Azotobacter vinelandii MoFe-protein, a position that was recently identified as the CO-binding site. The Se2B-labeled enzyme retains substrate reduction activity and marks the starting point for a crystallographic pulse-chase experiment of the active site during turnover. Through a series of crystal structures obtained at resolutions of 1.32-1.66 Å, including the CO-inhibited form of Av1-Se2B, the exchangeability of all three belt-sulfur sites is demonstrated, providing direct insights into unforeseen rearrangements of the metal center during catalysis.

PubMed: 26673079
DOI: 10.7554/eLife.11620

実験手法

X-RAY DIFFRACTION (1.53 Å)