1RW4

Nitrogenase Fe protein l127 deletion variant

1RW4 の概要

• エントリーDOI: 10.2210/pdb1rw4/pdb
• 分子名称: Nitrogenase iron protein 1, IRON/SULFUR CLUSTER, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: Azotobacter vinelandii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30017.78

構造登録者

Sen, S.,Igarashi, R.,Smith, A.,Johnson, M.K.,Seefeldt, L.C.,Peters, J.W. (登録日: 2003-12-15, 公開日: 2004-03-09, 最終更新日: 2023-08-23)

主引用文献

Sen, S.,Igarashi, R.,Smith, A.,Johnson, M.K.,Seefeldt, L.C.,Peters, J.W.
A Conformational Mimic of the MgATP-Bound "On State" of the Nitrogenase Iron Protein.
Biochemistry, 43:1787-1797, 2004

PubMed Abstract: The crystal structure of a nitrogenase Fe protein single site deletion variant reveals a distinctly new conformation of the Fe protein and indicates that, upon binding of MgATP, the Fe protein undergoes a dramatic conformational change that is largely manifested in the rigid-body reorientation of the homodimeric Fe protein subunits with respect to one another. The observed conformational state allows the rationalization of a model of structurally and chemically complementary interactions that occur upon initial complex formation with the MoFe protein component that are distinct from the protein-protein interactions that have been characterized previously for stabilized nitrogenase complexes. The crystallographic results, in combination with complementary UV-visible absorption, EPR, and resonance Raman spectroscopic data, indicate that the [4Fe-4S] cluster of both the Fe protein deletion variant and the native Fe protein in the presence of MgATP can reversibly cycle between a regular cubane-type [4Fe-4S] cluster in the reduced state and a cleaved form involving two [2Fe-2S] fragments in the oxidized state. Resonance Raman studies indicate that this novel cluster conversion is induced by glycerol, and the crystallographic data suggest that glycerol is bound as a bridging bidentate ligand to both [2Fe-2S] cluster fragments in the oxidized state.

PubMed: 14967020
DOI: 10.1021/bi0358465

実験手法

X-RAY DIFFRACTION (2.5 Å)