1f5v: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1f5v.jpg|left|200px]] | [[Image:1f5v.jpg|left|200px]] | ||
'''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 | ||
|PDB= 1f5v |SIZE=350|CAPTION= <scene name='initialview01'>1f5v</scene>, resolution 1.7Å | |||
|SITE= | |||
|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] | |||
|GENE= | |||
}} | |||
'''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== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1F5V is a [ | 1F5V is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F5V OCA]. | ||
==Reference== | ==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:[http:// | 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: NADPH dehydrogenase (quinone)]] | [[Category: NADPH dehydrogenase (quinone)]] | ||
| Line 28: | Line 37: | ||
[[Category: oxidoreduction]] | [[Category: oxidoreduction]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:04:51 2008'' | ||
Revision as of 09:04, 20 March 2008
| |||||||||||||
| 1f5v, resolution 1.7Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | FMN | ||||||||||||
| Activity: | NADPH dehydrogenase (quinone), with EC number 1.6.99.6 | ||||||||||||
| 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
Page seeded by OCA on Thu Mar 20 11:04:51 2008