1N2C

NITROGENASE COMPLEX FROM AZOTOBACTER VINELANDII STABILIZED BY ADP-TETRAFLUOROALUMINATE

1N2C の概要

• エントリーDOI: 10.2210/pdb1n2c/pdb
• 分子名称: NITROGENASE MOLYBDENUM-IRON PROTEIN, ADENOSINE-5'-DIPHOSPHATE, IRON/SULFUR CLUSTER, ... (11 entities in total)
• 機能のキーワード: nitrogenase, nitrogen fixation, signal transduction, electron transfer, atp hydrolysis, complex of nitrogenase proteins
• 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: 361248.21

構造登録者

Schindelin, H.,Kisker, C.,Rees, D.C. (登録日: 1997-05-02, 公開日: 1997-11-12, 最終更新日: 2024-05-22)

主引用文献

Schindelin, H.,Kisker, C.,Schlessman, J.L.,Howard, J.B.,Rees, D.C.
Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction.
Nature, 387:370-376, 1997

PubMed Abstract: The coupling of ATP hydrolysis to electron transfer by the enzyme nitrogenase during biological nitrogen fixation is an important example of a nucleotide-dependent transduction mechanism. The crystal structure has been determined for the complex between the Fe-protein and MoFe-protein components of nitrogenase stabilized by ADP x AIF4-, previously used as a nucleoside triphosphate analogue in nucleotide-switch proteins. The structure reveals that the dimeric Fe-protein has undergone substantial conformational changes. The beta-phosphate and AIF4- groups are stabilized through intersubunit contacts that are critical for catalysis and the redox centre is repositioned to facilitate electron transfer. Interactions in the nitrogenase complex have broad implications for signal and energy transduction mechanisms in multiprotein complexes.

PubMed: 9163420
DOI: 10.1038/387370a0

実験手法

X-RAY DIFFRACTION (3 Å)