5XMW

Selenomethionine-derivated ZHD

Summary for 5XMW

• Entry DOI: 10.2210/pdb5xmw/pdb
• Related: 5C8Z
• Descriptor: Zearalenone lactonase (2 entities in total)
• Functional Keywords: lactonase, hydrolase, alpha-beta fold, zearalenone degrade
• Biological source: Bionectria ochroleuca
• Total number of polymer chains: 2
• Total formula weight: 62694.47

Authors

Hu, X.J. (deposition date: 2017-05-16, release date: 2018-04-25, Last modification date: 2024-10-30)

Primary citation

Qi, Q.,Yang, W.J.,Zhou, H.J.,Ming, D.M.,Sun, K.L.,Xu, T.Y.,Hu, X.J.,Lv, H.
The structure of a complex of the lactonohydrolase zearalenone hydrolase with the hydrolysis product of zearalenone at 1.60 angstrom resolution
Acta Crystallogr F Struct Biol Commun, 73:376-381, 2017

PubMed Abstract: Zearalenone hydrolase (ZHD) is an α/β-hydrolase that detoxifies and degrades the lactone zearalenone (ZEN), a naturally occurring oestrogenic mycotoxin that contaminates crops. Several apoenzyme and enzyme-substrate complex structures have been reported in the resolution range 2.4-2.6 Å. However, the properties and mechanism of this enzyme are not yet fully understood. Here, a 1.60 Å resolution structure of a ZHD-product complex is reported which was determined from a C-terminally His-tagged ZHD crystal soaked with 2 mM ZEN for 30 min. It shows that after the lactone-bond cleavage, the phenol-ring region moves closer to residues Leu132, Tyr187 and Pro188, while the lactone-ring region barely moves. Comparisons of the ZHD-substrate and ZHD-product structures show that the hydrophilic interactions change, especially Trp183 N, which shifts from contacting O2 to O12', suggesting that Trp183 is responsible for the unidirectional translational movement of the phenol ring. This structure provides information on the final stage of the catalytic mechanism of zearalenone hydrolysis.

PubMed: 28695844
DOI: 10.1107/S2053230X17007713

Experimental method

X-RAY DIFFRACTION (3 Å)