4C5Y
Crystal structure of A. niger ochratoxinase
Summary for 4C5Y
| Entry DOI | 10.2210/pdb4c5y/pdb |
| Related | 4C5Z 4C60 4C65 |
| Descriptor | OCHRATOXINASE, ZINC ION (3 entities in total) |
| Functional Keywords | hydrolase, metal-dependent amidohydrolase, ochratoxin a hydrolysis, amidohydrolase superfamily |
| Biological source | ASPERGILLUS NIGER |
| Total number of polymer chains | 2 |
| Total formula weight | 93641.29 |
| Authors | Dobritzsch, D.,Wang, H.,Schneider, G.,Yu, S. (deposition date: 2013-09-17, release date: 2014-07-02, Last modification date: 2023-12-20) |
| Primary citation | Dobritzsch, D.,Wang, H.,Schneider, G.,Yu, S. Structural and Functional Characterization of Ochratoxinase, a Novel Mycotoxin Degrading Enzyme. Biochem.J., 462:441-, 2014 Cited by PubMed Abstract: 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. In the present paper we report the identification, characterization and crystal structure (at 2.2 Å) 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°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 homo-octameric enzyme folds into a two-domain structure characteristic of a metal dependent amidohydrolase, with a twisted TIM (triosephosphateisomerase)-barrel and a smaller β-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 centre. PubMed: 24947135DOI: 10.1042/BJ20140382 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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