4c65: Difference between revisions
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''' | ==Crystal structure of A. niger ochratoxinase== | ||
<StructureSection load='4c65' size='340' side='right' caption='[[4c65]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4c65]] is a 8 chain structure. 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> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c5y|4c5y]], [[4c5z|4c5z]], [[4c60|4c60]]</td></tr> | |||
<tr><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://www.rcsb.org/pdb/explore.do?structureId=4c65 RCSB], [http://www.ebi.ac.uk/pdbsum/4c65 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Dobritzsch, D.]] | |||
[[Category: Schneider, G.]] | |||
[[Category: Wang, H.]] | |||
[[Category: Yu, S.]] | |||
[[Category: Amidohydrolase superfamily]] | |||
[[Category: Hydrolase]] | |||
[[Category: Metal-dependent amidohydrolase]] | |||
[[Category: Ochratoxin a hydrolysis]] | |||
Revision as of 08:21, 2 July 2014
Crystal structure of A. niger ochratoxinase
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