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1f5v

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[[Image:1f5v.jpg|left|200px]]
[[Image:1f5v.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1f5v |SIZE=350|CAPTION= <scene name='initialview01'>1f5v</scene>, resolution 1.7&Aring;
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The line below this paragraph, containing "STRUCTURE_1f5v", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/NADPH_dehydrogenase_(quinone) NADPH dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.99.6 1.6.99.6] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1f5v| PDB=1f5v | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f5v OCA], [http://www.ebi.ac.uk/pdbsum/1f5v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f5v RCSB]</span>
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}}
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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]]
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[[Category: NADPH dehydrogenase (quinone)]]
 
[[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.]]
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[[Category: escherichia coli]]
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[[Category: Escherichia coli]]
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[[Category: flavoprotein]]
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[[Category: Flavoprotein]]
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[[Category: nitrocompound]]
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[[Category: Nitrocompound]]
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[[Category: nitroreductase]]
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[[Category: Nitroreductase]]
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[[Category: oxidoreduction]]
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[[Category: Oxidoreduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:56:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:16:30 2008''
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Revision as of 12:56, 2 May 2008

Image:1f5v.jpg

Template:STRUCTURE 1f5v

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

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