1v4b

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{{Seed}}
 
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[[Image:1v4b.png|left|200px]]
 
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==The crystal structure of AzoR (Azo Reductase) from Escherichia coli: Oxidized form==
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The line below this paragraph, containing "STRUCTURE_1v4b", creates the "Structure Box" on the page.
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<StructureSection load='1v4b' size='340' side='right'caption='[[1v4b]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1v4b]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V4B FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
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{{STRUCTURE_1v4b| PDB=1v4b | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1v4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v4b OCA], [https://pdbe.org/1v4b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v4b RCSB], [https://www.ebi.ac.uk/pdbsum/1v4b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v4b ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AZOR_ECOLI AZOR_ECOLI] Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. The enzyme can reduce ethyl red and methyl red, but is not able to convert sulfonated azo dyes.<ref>PMID:2168383</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v4/1v4b_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1v4b ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===The crystal structure of AzoR (Azo Reductase) from Escherichia coli: Oxidized form===
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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<ref>PMID:16684776</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1v4b" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16684776 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16684776}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1V4B is a 1 chain 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].
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==Reference==
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<ref group="xtra">PMID:16684776</ref><references group="xtra"/>
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[[Category: Azobenzene reductase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Ito, K.]]
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[[Category: Large Structures]]
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[[Category: Tanokura, M.]]
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[[Category: Ito K]]
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[[Category: Azo reductase]]
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[[Category: Tanokura M]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 14:53:02 2009''
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Current revision

The crystal structure of AzoR (Azo Reductase) from Escherichia coli: Oxidized form

PDB ID 1v4b

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