5XWZ

Crystal structure of a lactonase from Cladophialophora bantiana

5XWZ の概要

• エントリーDOI: 10.2210/pdb5xwz/pdb
• 分子名称: Unplaced genomic scaffold supercont1.36, whole genome shotgun sequence, SODIUM ION, MALONATE ION, ... (5 entities in total)
• 機能のキーワード: alpha/beta-hydrolase, lactonase, zearalenone, hydrolase
• 由来する生物種: Cladophialophora bantiana CBS 173.52
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 120307.00

構造登録者

Zheng, Y.Y.,Liu, W.T.,Liu, W.D.,Chen, C.C.,Guo, R.T. (登録日: 2017-06-30, 公開日: 2018-05-02, 最終更新日: 2023-11-22)

主引用文献

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

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: 28876230
DOI: 10.1107/S2053230X17011840

実験手法

X-RAY DIFFRACTION (1.75 Å)