1M1N

Nitrogenase MoFe protein from Azotobacter vinelandii

1M1N の概要

• エントリーDOI: 10.2210/pdb1m1n/pdb
• 関連するPDBエントリー: 1n2c 2min 3min
• 分子名称: Nitrogenase molybdenum-iron protein alpha chain, Nitrogenase molybdenum-iron protein beta chain, 3-HYDROXY-3-CARBOXY-ADIPIC ACID, ... (7 entities in total)
• 機能のキーワード: atomic resolution, femo cofactor, nitrogen fixation, central nitrogen ligand, 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: 465373.69

構造登録者

Einsle, O.,Tezcan, F.A.,Andrade, S.L.A.,Schmid, B.,Yoshida, M.,Howard, J.B.,Rees, D.C. (登録日: 2002-06-19, 公開日: 2002-09-11, 最終更新日: 2024-02-14)

主引用文献

Einsle, O.,Tezcan, F.A.,Andrade, S.L.,Schmid, B.,Yoshida, M.,Howard, J.B.,Rees, D.C.
Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor.
Science, 297:1696-1700, 2002

PubMed Abstract: A high-resolution crystallographic analysis of the nitrogenase MoFe-protein reveals a previously unrecognized ligand coordinated to six iron atoms in the center of the catalytically essential FeMo-cofactor. The electron density for this ligand is masked in structures with resolutions lower than 1.55 angstroms, owing to Fourier series termination ripples from the surrounding iron and sulfur atoms in the cofactor. The central atom completes an approximate tetrahedral coordination for the six iron atoms, instead of the trigonal coordination proposed on the basis of lower resolution structures. The crystallographic refinement at 1.16 angstrom resolution is consistent with this newly detected component being a light element, most plausibly nitrogen. The presence of a nitrogen atom in the cofactor would have important implications for the mechanism of dinitrogen reduction by nitrogenase.

PubMed: 12215645
DOI: 10.1126/science.1073877

実験手法

X-RAY DIFFRACTION (1.16 Å)