5XWZ
Crystal structure of a lactonase from Cladophialophora bantiana
Summary for 5XWZ
| Entry DOI | 10.2210/pdb5xwz/pdb |
| Descriptor | Unplaced genomic scaffold supercont1.36, whole genome shotgun sequence, SODIUM ION, MALONATE ION, ... (5 entities in total) |
| Functional Keywords | alpha/beta-hydrolase, lactonase, zearalenone, hydrolase |
| Biological source | Cladophialophora bantiana CBS 173.52 |
| Total number of polymer chains | 4 |
| Total formula weight | 120307.00 |
| Authors | Zheng, Y.Y.,Liu, W.T.,Liu, W.D.,Chen, C.C.,Guo, R.T. (deposition date: 2017-06-30, release date: 2018-05-02, Last modification date: 2023-11-22) |
| Primary citation | Hui, R.,Hu, X.,Liu, W.,Liu, W.,Zheng, Y.,Chen, Y.,Guo, R.T.,Jin, J.,Chen, C.C. Characterization and crystal structure of a novel zearalenone hydrolase from Cladophialophora bantiana Acta Crystallogr F Struct Biol Commun, 73:515-519, 2017 Cited by PubMed Abstract: Zearalenone (ZEN) is a mycotoxin which causes huge economic losses in the food and animal feed industries. The lactonase ZHD101 from Clonostachys rosea, which catalyzes the hydrolytic degradation of ZEN, is the only known ZEN-detoxifying enzyme. Here, a protein homologous to ZHD101, denoted CbZHD, from Cladophialophora batiana was expressed and characterized. Sequence alignment indicates that CbZHD possesses the same catalytic triad and ZEN-interacting residues as found in ZHD101. CbZHD exhibits optimal enzyme activity at 35°C and pH 8, and is sensitive to heat treatment. The crystal structure of apo CbZHD was determined to 1.75 Å resolution. The active-site compositions of CbZHD and ZHD101 were analyzed. PubMed: 28876230DOI: 10.1107/S2053230X17011840 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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