5xfa | pdb_00005xfa

Crystal structure of NAD+-reducing [NiFe]-hydrogenase in the H2-reduced state

spinqualitylabelsall models 5xfa, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5xfa is a 8 chain structure with sequence from Hydrogenophilus thermoluteolus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: FCO, FES, MG, NI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A077L6X8_HYDTE Publication Abstract from PubMed NAD+ (oxidized form of NAD:nicotinamide adenine dinucleotide)-reducing soluble [NiFe]-hydrogenase (SH) is phylogenetically related to NADH (reduced form of NAD+):quinone oxidoreductase (complex I), but the geometrical arrangements of the subunits and Fe-S clusters are unclear. Here, we describe the crystal structures of SH in the oxidized and reduced states. The cluster arrangement is similar to that of complex I, but the subunits orientation is not, which supports the hypothesis that subunits evolved as prebuilt modules. The oxidized active site includes a six-coordinate Ni, which is unprecedented for hydrogenases, whose coordination geometry would prevent O2 from approaching. In the reduced state showing the normal active site structure without a physiological electron acceptor, the flavin mononucleotide cofactor is dissociated, which may be caused by the oxidation state change of nearby Fe-S clusters and may suppress production of reactive oxygen species. Structural basis of the redox switches in the NAD+-reducing soluble [NiFe]-hydrogenase.,Shomura Y, Taketa M, Nakashima H, Tai H, Nakagawa H, Ikeda Y, Ishii M, Igarashi Y, Nishihara H, Yoon KS, Ogo S, Hirota S, Higuchi Y Science. 2017 Sep 1;357(6354):928-932. doi: 10.1126/science.aan4497. PMID:28860386 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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