6q93

MgADP-bound Fe protein of Vanadium nitrogenase from Azotobacter vinelandii

spinqualitylabelsall models 6q93, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6q93 is a 8 chain structure with sequence from Azotobacter vinelandii DJ. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: ADP, MG, SF4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C1DI30_AZOVD The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.[HAMAP-Rule:MF_00533] Publication Abstract from PubMed Nitrogenases catalyze the biological fixation of inert N2 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 A 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. Crystal structure of VnfH, the iron protein component of vanadium nitrogenase.,Rohde M, Trncik C, Sippel D, Gerhardt S, Einsle O J Biol Inorg Chem. 2018 Oct;23(7):1049-1056. doi: 10.1007/s00775-018-1602-4. Epub, 2018 Aug 23. PMID:30141094 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Nitrogenase 3D structures

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