1bkj | pdb_00001bkj

NADPH:FMN OXIDOREDUCTASE FROM VIBRIO HARVEYI

spinqualitylabelsall models 1bkj, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1bkj is a 2 chain structure with sequence from "achromobacter_harveyi"_johnson_and_shunk_1936 "achromobacter harveyi" johnson and shunk 1936. This structure supersedes the now removed PDB entry 1cum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FMN, PO4 Gene: VIBRIO HARVEYI NADPH\:FMN OXIDOREDUCTASE ("Achromobacter harveyi" Johnson and Shunk 1936) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FRP_VIBHA] Involved in bioluminescence. It is a good supplier of reduced flavin mononucleotide (FMNH2) to the bioluminescence reaction. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed We report the structure of an NADPH:FMN oxidoreductase (flavin reductase P) that is involved in bioluminescence by providing reduced FMN to luciferase. The 1.8 A crystal structure of flavin reductase P from Vibrio harveyi was solved by multiple isomorphous replacement and reveals that the enzyme is a unique dimer of interlocking subunits, with 9352 A2 of surface area buried in the dimer interface. Each subunit comprises two domains. The first domain consists of a four-stranded antiparallel beta-sheet flanked by helices on either side. The second domain reaches out from one subunit and embraces the other subunit and is responsible for interlocking the two subunits. Our structure explains why flavin reductase P is specific for FMN as cofactor. FMN is recognized and tightly bound by a network of 16 hydrogen bonds, while steric considerations prevent the binding of FAD. A flexible loop containing a Lys and an Arg could account for the NADPH specificity. The structure reveals information about several aspects of the catalytic mechanism. For example, we show that the first step in catalysis, which is hydride transfer from C4 of NADPH to cofactor FMN, involves addition to the re face of the FMN, probably at the N5 position. The limited accessibility of the FMN binding pocket and the extensive FMN-protein hydrogen bond network are consistent with the observed ping-pong bisubstrate--biproduct reaction kinetics. Finally, we propose a model for how flavin reductase P might shuttle electrons between NADPH and luciferase. Flavin reductase P: structure of a dimeric enzyme that reduces flavin.,Tanner JJ, Lei B, Tu SC, Krause KL Biochemistry. 1996 Oct 22;35(42):13531-9. PMID:8885832 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Flavin reductase

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