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3lt5

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{{Seed}}
 
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[[Image:3lt5.jpg|left|200px]]
 
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==X-ray Crystallographic structure of a Pseudomonas Aeruginosa Azoreductase in complex with balsalazide==
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The line below this paragraph, containing "STRUCTURE_3lt5", creates the "Structure Box" on the page.
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<StructureSection load='3lt5' size='340' side='right'caption='[[3lt5]], [[Resolution|resolution]] 2.30&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'>[[3lt5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LT5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LT5 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.3&#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=BLQ:(3E)-3-({4-[(2-CARBOXYETHYL)CARBAMOYL]PHENYL}HYDRAZONO)-6-OXOCYCLOHEXA-1,4-DIENE-1-CARBOXYLIC+ACID'>BLQ</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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{{STRUCTURE_3lt5| PDB=3lt5 | 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=3lt5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lt5 OCA], [https://pdbe.org/3lt5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lt5 RCSB], [https://www.ebi.ac.uk/pdbsum/3lt5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lt5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AZOR1_PSEAE AZOR1_PSEAE] 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 (By similarity).
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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/lt/3lt5_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=3lt5 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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Azoreductases are important due to their ability to activate anti-inflammatory azo pro-drugs and to detoxify azo dyes. Three genes encoding azoreductases have been identified in Pseudomonas aeruginosa. We describe here a comparison of the three enzymes. The pure recombinant proteins each have a distinct substrate specificity profile against a range of azo substrates. Using the structure of P. aeruginosa azoreductase (paAzoR) 1 and the homology models of paAzoR2 and paAzoR3, we have identified residues important for substrate specificity. We have defined a novel flavin mononucleotide binding cradle, which is a recurrent motif in many flavodoxin-like proteins. A novel structure of paAzoR1 with the azo pro-drug balsalazide bound within the active site was determined by X-ray crystallography and demonstrates that the substrate is present in a hydrazone tautomer conformation. We propose that the structure with balsalazide bound represents an enzyme intermediate and, together with the flavin mononucleotide binding cradle, we propose a novel catalytic mechanism.
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===X-ray Crystallographic structure of a Pseudomonas Aeruginosa Azoreductase in complex with balsalazide===
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A novel mechanism for azoreduction.,Ryan A, Laurieri N, Westwood I, Wang CJ, Lowe E, Sim E J Mol Biol. 2010 Jul 2;400(1):24-37. Epub 2010 Apr 24. PMID:20417637<ref>PMID:20417637</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>
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The line below this paragraph, {{ABSTRACT_PUBMED_20417637}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3lt5" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20417637 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20417637}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3LT5 is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LT5 OCA].
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[[Category: Pseudomonas aeruginosa PAO1]]
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[[Category: Laurieri N]]
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==Reference==
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[[Category: Lowe E]]
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<ref group="xtra">PMID:20417637</ref><references group="xtra"/>
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[[Category: Ryan A]]
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Sim E]]
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[[Category: Laurieri, N.]]
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[[Category: Wang C-J]]
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[[Category: Lowe, E.]]
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[[Category: Westwood I]]
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[[Category: Ryan, A.]]
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[[Category: Sim, E.]]
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[[Category: Wang, C J.]]
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[[Category: Westwood, I.]]
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[[Category: Azoreductase]]
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[[Category: Balsalazide]]
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[[Category: Flavoprotein]]
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[[Category: Fmn]]
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[[Category: Hydrazo]]
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[[Category: Inflammatory bowel disease]]
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[[Category: Oxidoreductase]]
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[[Category: P. aeruginosa]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 12 11:02:37 2010''
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Current revision

X-ray Crystallographic structure of a Pseudomonas Aeruginosa Azoreductase in complex with balsalazide

PDB ID 3lt5

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