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1f5v

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Image:1f5v.jpg

1f5v, resolution 1.7Å

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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

Overview

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.

About this Structure

1F5V is a Single protein structure of sequence from Escherichia coli with FMN as ligand. Active as NADPH dehydrogenase (quinone), with EC number 1.6.99.6 Full crystallographic information is available from OCA.

Reference

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

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