1f5v: Difference between revisions

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[[Image:1f5v.jpg|left|200px]]<br /><applet load="1f5v" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1f5v.jpg|left|200px]]
caption="1f5v, resolution 1.7&Aring;" />
 
'''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'''<br />
{{Structure
|PDB= 1f5v |SIZE=350|CAPTION= <scene name='initialview01'>1f5v</scene>, resolution 1.7&Aring;
|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==
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==About this Structure==
==About this Structure==
1F5V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=FMN:'>FMN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F5V OCA].  
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=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: NADPH dehydrogenase (quinone)]]
[[Category: NADPH dehydrogenase (quinone)]]
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[[Category: oxidoreduction]]
[[Category: oxidoreduction]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:11 2008''
''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

File:1f5v.jpg


Drag the structure with the mouse to rotate
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

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