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4c65

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Crystal structure of A. niger ochratoxinase

Structural highlights

4c65 is a 8 chain structure with sequence from Aspergillus niger. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[1] ^[2]

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Dobritzsch D, Wang H, Schneider G, Yu S. Structural and functional characterization of ochratoxinase, a novel mycotoxin degrading enzyme. Biochem J. 2014 Jun 20. PMID:24947135 doi:http://dx.doi.org/10.1042/BJ20140382
↑ Xiong K, Liu J, Wang X, Sun B, Zhang Y, Zhao Z, Pei P, Li X. Engineering a carboxypeptidase from Aspergillus niger M00988 by mutation to increase its ability in high Fischer ratio oligopeptide preparation. J Biotechnol. 2021 Mar 20;330:1-8. doi: 10.1016/j.jbiotec.2021.02.015. Epub 2021 , Feb 26. PMID:33647354 doi:http://dx.doi.org/10.1016/j.jbiotec.2021.02.015
↑ Dobritzsch D, Wang H, Schneider G, Yu S. Structural and functional characterization of ochratoxinase, a novel mycotoxin degrading enzyme. Biochem J. 2014 Jun 20. PMID:24947135 doi:http://dx.doi.org/10.1042/BJ20140382

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4c65"

@@ Line 3: / Line 3: @@
 <StructureSection load='4c65' size='340' side='right'caption='[[4c65]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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>
+<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>
 </table>
+== Function ==
+[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: A. niger]]
+[[Category: Aspergillus niger]]
 [[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]]

4c65

From Proteopedia

Current revision

Crystal structure of A. niger ochratoxinase

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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