2AFH

Crystal Structure of Nucleotide-Free Av2-Av1 Complex

2AFH の概要

• エントリーDOI: 10.2210/pdb2afh/pdb
• 関連するPDBエントリー: 2AFI 2AFK
• 分子名称: Nitrogenase molybdenum-iron protein, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, TETRAETHYLENE GLYCOL, ... (16 entities in total)
• 機能のキーワード: nitrogen fixation, iron-sulfur, metal-binding, molybdenum, oxidoreductase
• 由来する生物種: Azotobacter vinelandii; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 298806.93

構造登録者

Tezcan, F.A.,Kaiser, J.T.,Mustafi, D.,Walton, M.Y.,Howard, J.B.,Rees, D.C. (登録日: 2005-07-25, 公開日: 2005-09-06, 最終更新日: 2023-08-23)

主引用文献

Tezcan, F.A.,Kaiser, J.T.,Mustafi, D.,Walton, M.Y.,Howard, J.B.,Rees, D.C.
Nitrogenase Complexes: Multiple Docking Sites for a Nucleotide Switch Protein
Science, 309:1377-1380, 2005

PubMed Abstract: Adenosine triphosphate (ATP) hydrolysis in the nitrogenase complex controls the cycle of association and dissociation between the electron donor adenosine triphosphatase (ATPase) (Fe-protein) and its target catalytic protein (MoFe-protein), driving the reduction of dinitrogen into ammonia. Crystal structures in different nucleotide states have been determined that identify conformational changes in the nitrogenase complex during ATP turnover. These structures reveal distinct and mutually exclusive interaction sites on the MoFe-protein surface that are selectively populated, depending on the Fe-protein nucleotide state. A consequence of these different docking geometries is that the distance between redox cofactors, a critical determinant of the intermolecular electron transfer rate, is coupled to the nucleotide state. More generally, stabilization of distinct docking geometries by different nucleotide states, as seen for nitrogenase, could enable nucleotide hydrolysis to drive the relative motion of protein partners in molecular motors and other systems.

PubMed: 16123301
DOI: 10.1126/science.1115653

実験手法

X-RAY DIFFRACTION (2.1 Å)