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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''' | '''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''' | ||
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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., 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:[http://www.ncbi.nlm.nih.gov/pubmed/11034992 11034992] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11034992 11034992] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Kobori, T.]] | [[Category: Kobori, T.]] | ||
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[[Category: Tanokura, M.]] | [[Category: Tanokura, M.]] | ||
[[Category: Zenno, S.]] | [[Category: Zenno, S.]] | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Flavoprotein]] | ||
[[Category: | [[Category: Nitrocompound]] | ||
[[Category: | [[Category: Nitroreductase]] | ||
[[Category: | [[Category: Oxidoreduction]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:56:22 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 12:56, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 15:56:22 2008
