1f5v: Difference between revisions
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|PDB= 1f5v |SIZE=350|CAPTION= <scene name='initialview01'>1f5v</scene>, resolution 1.7Å | |PDB= 1f5v |SIZE=350|CAPTION= <scene name='initialview01'>1f5v</scene>, resolution 1.7Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=FMN:FLAVIN MONONUCLEOTIDE'>FMN</scene> | |LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene> | ||
|ACTIVITY= [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] | |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> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|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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[[Category: Tanokura, M.]] | [[Category: Tanokura, M.]] | ||
[[Category: Zenno, S.]] | [[Category: Zenno, S.]] | ||
[[Category: escherichia coli]] | [[Category: escherichia coli]] | ||
[[Category: flavoprotein]] | [[Category: flavoprotein]] | ||
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[[Category: oxidoreduction]] | [[Category: oxidoreduction]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:16:30 2008'' | ||
Revision as of 17:16, 30 March 2008
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| 1f5v, resolution 1.7Å | |||||||||||||
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| Ligands: | FMN | ||||||||||||
| Activity: | NADPH dehydrogenase (quinone), with EC number 1.6.99.6 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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