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1v4b
From Proteopedia
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|PDB= 1v4b |SIZE=350|CAPTION= <scene name='initialview01'>1v4b</scene>, resolution 1.80Å | |PDB= 1v4b |SIZE=350|CAPTION= <scene name='initialview01'>1v4b</scene>, resolution 1.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1v4c|1V4C]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v4b OCA], [http://www.ebi.ac.uk/pdbsum/1v4b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v4b RCSB]</span> | ||
}} | }} | ||
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[[Category: Ito, K.]] | [[Category: Ito, K.]] | ||
[[Category: Tanokura, M.]] | [[Category: Tanokura, M.]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: FMN]] | ||
| - | [[Category: IPA]] | ||
[[Category: azo reductase]] | [[Category: azo reductase]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:19:20 2008'' |
Revision as of 21:19, 30 March 2008
| |||||||
| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Azobenzene reductase, with EC number 1.7.1.6 | ||||||
| Related: | 1V4C
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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