6Q93

MgADP-bound Fe protein of Vanadium nitrogenase from Azotobacter vinelandii

6Q93 の概要

• エントリーDOI: 10.2210/pdb6q93/pdb
• 分子名称: Nitrogenase iron protein, IRON/SULFUR CLUSTER, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: biological nitrogen fixation, dinitrogenase reductase, vanadium nitrogenase, fe protein, vnfh, electron transport
• 由来する生物種: Azotobacter vinelandii (strain DJ / ATCC BAA-1303)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 253552.71

構造登録者

Rohde, M.,Gerhardt, S.,Einsle, O. (登録日: 2018-12-17, 公開日: 2019-02-27, 最終更新日: 2024-01-24)

主引用文献

Rohde, M.,Trncik, C.,Sippel, D.,Gerhardt, S.,Einsle, O.
Crystal structure of VnfH, the iron protein component of vanadium nitrogenase.
J. Biol. Inorg. Chem., 23:1049-1056, 2018

PubMed Abstract: Nitrogenases catalyze the biological fixation of inert N into bioavailable ammonium. They are bipartite systems consisting of the catalytic dinitrogenase and a complementary reductase, the Fe protein that is also the site where ATP is hydrolyzed to drive the reaction forward. Three different subclasses of dinitrogenases are known, employing either molybdenum, vanadium or only iron at their active site cofactor. Although in all these classes the mode and mechanism of interaction with Fe protein is conserved, each one encodes its own orthologue of the reductase in the corresponding gene cluster. Here we present the 2.2 Å resolution structure of VnfH from Azotobacter vinelandii, the Fe protein of the alternative, vanadium-dependent nitrogenase system, in its ADP-bound state. VnfH adopts the same conformation that was observed for NifH, the Fe protein of molybdenum nitrogenase, in complex with ADP, representing a state of the functional cycle that is ready for reduction and subsequent nucleotide exchange. The overall similarity of NifH and VnfH confirms the experimentally determined cross-reactivity of both ATP-hydrolyzing reductases.

PubMed: 30141094
DOI: 10.1007/s00775-018-1602-4

実験手法

X-RAY DIFFRACTION (2.2 Å)