4c65: Difference between revisions

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<StructureSection load='4c65' size='340' side='right'caption='[[4c65]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='4c65' size='340' side='right'caption='[[4c65]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4c65]] is a 8 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=4C65 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C65 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4c65]] is a 8 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=4C65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C65 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c5y|4c5y]], [[4c5z|4c5z]], [[4c60|4c60]]</td></tr>
</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=4c65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c65 OCA], [https://pdbe.org/4c65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c65 RCSB], [https://www.ebi.ac.uk/pdbsum/4c65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c65 ProSAT]</span></td></tr>
<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=4c65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c65 OCA], [http://pdbe.org/4c65 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c65 RCSB], [http://www.ebi.ac.uk/pdbsum/4c65 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c65 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[[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>  
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.
 
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4c65" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: A. niger]]
[[Category: Aspergillus niger]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Dobritzsch, D]]
[[Category: Dobritzsch D]]
[[Category: Schneider, G]]
[[Category: Schneider G]]
[[Category: Wang, H]]
[[Category: Wang H]]
[[Category: Yu, S]]
[[Category: Yu S]]
[[Category: Amidohydrolase superfamily]]
[[Category: Hydrolase]]
[[Category: Metal-dependent amidohydrolase]]
[[Category: Ochratoxin a hydrolysis]]

Revision as of 17:28, 7 September 2022

Crystal structure of A. niger ochratoxinase

4c65, resolution 2.20Å

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