4c0w
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4c0w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C0W FirstGlance]. <br> | <table><tr><td colspan='2'>[[4c0w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C0W FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4c0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c0w OCA], [https://pdbe.org/4c0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c0w RCSB], [https://www.ebi.ac.uk/pdbsum/4c0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c0w ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4c0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c0w OCA], [https://pdbe.org/4c0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c0w RCSB], [https://www.ebi.ac.uk/pdbsum/4c0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c0w ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/AZOR1_PSEPK AZOR1_PSEPK] 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). | |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Enzymatic degradation of azo dyes begins with the reduction of the azo bond. In this paper we report the crystal structures of the native azoreductase from Pseudomonas putida MET94 (PpAzoR) (1.60 A), of PpAzoR in complex with the anthraquinone-2-sulfonate (1.50 A) and of PpAzoR in complex with Reactive Black 5 dye (1.90 A). These structures reveal the residues and subtle changes that accompany substrate binding and release. Such changes highlight the fine control of access to the catalytic site that is required by the ping-pong mechanism, and in turn the specificity offered by the enzyme towards different substrates. The topology surrounding the active site shows novel features of substrate recognition and binding that help to explain and differentiate the substrate specificity observed among different bacterial azoreductases. This article is protected by copyright. All rights reserved. | ||
| + | |||
| + | The Crystal Structure of Pseudomonas putida AzoR: the active site revisited.,Goncalves AM, Mendes S, de Sanctis D, Martins LO, Bento I FEBS J. 2013 Oct 16. doi: 10.1111/febs.12568. PMID:24127652<ref>PMID:24127652</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4c0w" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
The crystal strucuture of native PpAzoR
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