1v4b: Difference between revisions
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[[Image:1v4b.gif|left|200px]] | [[Image:1v4b.gif|left|200px]] | ||
'''The crystal structure of AzoR (Azo Reductase) from Escherichia coli: Oxidized form''' | {{Structure | ||
|PDB= 1v4b |SIZE=350|CAPTION= <scene name='initialview01'>1v4b</scene>, resolution 1.80Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> and <scene name='pdbligand=IPA:ISOPROPYL ALCOHOL'>IPA</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Azobenzene_reductase Azobenzene reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.1.6 1.7.1.6] | |||
|GENE= | |||
}} | |||
'''The crystal structure of AzoR (Azo Reductase) from Escherichia coli: Oxidized form''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1V4B is a [ | 1V4B 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=1V4B OCA]. | ||
==Reference== | ==Reference== | ||
Three-dimensional structure of AzoR from Escherichia coli. An oxidereductase conserved in microorganisms., Ito K, Nakanishi M, Lee WC, Sasaki H, Zenno S, Saigo K, Kitade Y, Tanokura M, J Biol Chem. 2006 Jul 21;281(29):20567-76. Epub 2006 May 9. PMID:[http:// | Three-dimensional structure of AzoR from Escherichia coli. An oxidereductase conserved in microorganisms., Ito K, Nakanishi M, Lee WC, Sasaki H, Zenno S, Saigo K, Kitade Y, Tanokura M, J Biol Chem. 2006 Jul 21;281(29):20567-76. Epub 2006 May 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16684776 16684776] | ||
[[Category: Azobenzene reductase]] | [[Category: Azobenzene reductase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''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 14:40:41 2008'' | ||
Revision as of 12:40, 20 March 2008
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| 1v4b, resolution 1.80Å | |||||||||||||
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| Ligands: | FMN, EDO and IPA | ||||||||||||
| Activity: | Azobenzene reductase, with EC number 1.7.1.6 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
The crystal structure of AzoR (Azo Reductase) from Escherichia coli: Oxidized form
Overview
The crystal structure of AzoR (azoreductase) has been determined in complex with FMN for two different crystal forms at 1.8 and 2.2 A resolution. AzoR is an oxidoreductase isolated from Escherichia coli as a protein responsible for the degradation of azo compounds. This enzyme is an FMN-dependent NADH-azoreductase and catalyzes the reductive cleavage of azo groups by a ping-pong mechanism. The structure suggests that AzoR acts in a homodimeric state forming the two identical catalytic sites to which both monomers contribute. The structure revealed that each monomer of AzoR has a flavodoxin-like structure, without the explicit overall amino acid sequence homology. Superposition of the structures from the two different crystal forms revealed the conformational change and suggested a mechanism for accommodating substrates of different size. Furthermore, comparison of the active site structure with that of NQO1 complexed with substrates provides clues to the possible substrate-binding mechanism of AzoR.
About this Structure
1V4B is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of AzoR from Escherichia coli. An oxidereductase conserved in microorganisms., Ito K, Nakanishi M, Lee WC, Sasaki H, Zenno S, Saigo K, Kitade Y, Tanokura M, J Biol Chem. 2006 Jul 21;281(29):20567-76. Epub 2006 May 9. PMID:16684776
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