1RW4
Nitrogenase Fe protein l127 deletion variant
Summary for 1RW4
| Entry DOI | 10.2210/pdb1rw4/pdb |
| Descriptor | Nitrogenase iron protein 1, IRON/SULFUR CLUSTER, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | oxidoreductase |
| Biological source | Azotobacter vinelandii |
| Total number of polymer chains | 1 |
| Total formula weight | 30017.78 |
| Authors | Sen, S.,Igarashi, R.,Smith, A.,Johnson, M.K.,Seefeldt, L.C.,Peters, J.W. (deposition date: 2003-12-15, release date: 2004-03-09, Last modification date: 2023-08-23) |
| Primary citation | 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 Cited by 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: 14967020DOI: 10.1021/bi0358465 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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