4c5y

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<StructureSection load='4c5y' size='340' side='right'caption='[[4c5y]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='4c5y' size='340' side='right'caption='[[4c5y]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4c5y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/A._niger A. niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C5Y FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4c5y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C5Y FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr>
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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=4c5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5y OCA], [https://pdbe.org/4c5y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c5y RCSB], [https://www.ebi.ac.uk/pdbsum/4c5y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c5y ProSAT]</span></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c5z|4c5z]], [[4c60|4c60]], [[4c65|4c65]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4c5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5y OCA], [http://pdbe.org/4c5y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c5y RCSB], [http://www.ebi.ac.uk/pdbsum/4c5y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c5y ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[[https://www.uniprot.org/uniprot/OTASE_ASPNC OTASE_ASPNC]] Carboxypeptidase that catalyzes the release of a C-terminal amino acid with specific catalytic activity for aromatic amino acids such as phenylalanine (PubMed:24947135, PubMed:33647354). Is able to degrade ochratoxin A, one of the five major mycotoxins most harmful to humans and animals that is produced by Aspergillus and Penicillium species and occurs in a wide range of agricultural products (PubMed:24947135).<ref>PMID:24947135</ref> <ref>PMID:33647354</ref>
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Ochratoxin, with ochratoxin A as the dominant form, is one of the five major mycotoxins most harmful to humans and animals. It is produced by Aspergillus and Penicillium species and occurs in a wide range of agricultural products. Detoxification of contaminated food is a challenging health issue. Here we report the identification, characterization and crystal structure (at 2.2 A) of a novel, microbial ochratoxinase from Aspergillus niger. A putative amidase gene encoding a 480 amino acid polypeptide was cloned and homologously expressed in A. niger. The recombinant protein is N-terminally truncated, thermostable, has optimal activity at pH~6 and 66 degrees C, and is more efficient in ochratoxin A hydrolysis than carboxypeptidase A and Y, the two previously known enzymes capable of degrading this mycotoxin. The subunit of the homooctameric enzyme folds into a two-domain structure characteristic for a metal dependent amidohydrolase, with a twisted TIM-barrel and a smaller b-sandwich domain. The active site contains an aspartate residue for acid-base catalysis, and a carboxylated lysine and four histidine residues for binding of a binuclear metal center.
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Structural and functional characterization of ochratoxinase, a novel mycotoxin degrading enzyme.,Dobritzsch D, Wang H, Schneider G, Yu S Biochem J. 2014 Jun 20. PMID:24947135<ref>PMID:24947135</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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<div class="pdbe-citations 4c5y" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: A. niger]]
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[[Category: Aspergillus niger]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Dobritzsch, D]]
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[[Category: Dobritzsch D]]
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[[Category: Schneider, G]]
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[[Category: Schneider G]]
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[[Category: Wang, H]]
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[[Category: Wang H]]
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[[Category: Yu, S]]
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[[Category: Yu S]]
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[[Category: Amidohydrolase superfamily]]
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[[Category: Hydrolase]]
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[[Category: Metal-dependent amidohydrolase]]
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[[Category: Ochratoxin a hydrolysis]]
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Revision as of 17:28, 7 September 2022

Crystal structure of A. niger ochratoxinase

PDB ID 4c5y

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