1f5v | pdb_00001f5v

STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF A FLAVOPROTEIN FROM ESCHERICHIA COLI THAT REDUCES NITROCOMPOUNDS. ALTERATION OF PYRIDINE NUCLEOTIDE BINDING BY A SINGLE AMINO ACID SUBSTITUTION

spinqualitylabelsall models 1f5v, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1f5v is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FMN Activity: NADPH dehydrogenase (quinone), with EC number 1.6.5.10 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NFSA_ECOLI] Reduction of nitroaromatic compounds using NADH. Reduces nitrofurazone by a ping-pong bi-bi mechanism possibly to generate a two-electron transfer product. Major component of the oxygen-insensitive nitroreductase activity in E.coli. 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 The crystal structure of a major oxygen-insensitive nitroreductase (NfsA) from Escherichia coli has been solved by the molecular replacement method at 1.7-A resolution. This enzyme is a homodimeric flavoprotein with one FMN cofactor per monomer and catalyzes reduction of nitrocompounds using NADPH. The structure exhibits an alpha + beta-fold, and is comprised of a central domain and an excursion domain. The overall structure of NfsA is similar to the NADPH-dependent flavin reductase of Vibrio harveyi, despite definite difference in the spatial arrangement of residues around the putative substrate-binding site. On the basis of the crystal structure of NfsA and its alignment with the V. harveyi flavin reductase and the NADPH-dependent nitro/flavin reductase of Bacillus subtilis, residues Arg(203) and Arg(208) of the loop region between helices I and J in the vicinity of the catalytic center FMN is predicted as a determinant for NADPH binding. The R203A mutant results in a 33-fold increase in the K(m) value for NADPH indicating that the side chain of Arg(203) plays a key role in binding NADPH possibly to interact with the 2'-phosphate group. Structure and site-directed mutagenesis of a flavoprotein from Escherichia coli that reduces nitrocompounds: alteration of pyridine nucleotide binding by a single amino acid substitution.,Kobori T, Sasaki H, Lee WC, Zenno S, Saigo K, Murphy ME, Tanokura M J Biol Chem. 2001 Jan 26;276(4):2816-23. Epub 2000 Oct 16. PMID:11034992 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Nitroreductase

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