Peng_2014_RSC.Adv_4_62321

Reference

Title : Crystal structure and substrate-binding mode of the mycoestrogen-detoxifying lactonase ZHD from Clonostachys rosea - Peng_2014_RSC.Adv_4_62321
Author(s) : Peng W , Ko TP , Yang YY , Zheng YY , Chen CC , Zhu Z , Huang CH , Zeng YF , Huang JW , Wang AHJ , Liu JR , Guo RT
Ref : RSC Advances , 4 :62321 , 2014
Abstract :

The mycotoxin zearalenone has been contaminating maize and other grains. It can be hydrolyzed and inactivated by the lactonase ZHD, which belongs to the alpha/beta-hydrolase family. Besides the catalytic core domain, the enzyme comprises an alpha-helical cap domain. Zearalenone differs from other quorum-sensing lactones in its chemical structure. As revealed by the complex structure, the substrate binds into a deep pocket between the core and cap domains, adjacent to the catalytic triad Ser102-His242-Glu126. The enzyme-substrate interactions include three direct hydrogen bonds and several nonpolar contacts. In particular, the Trp183 side chain is engaged in both hydrogen bonding and T-stacking interactions with the benzoate ring. The central role of Trp183 in substrate binding was verified by the mutants W183A, W183H and W183F. Several mutants were also produced to investigate the roles of nearby amino-acid residues. Interestingly, mutants that destabilize the dimer had adverse functional effects on ZHD.

PubMedSearch : Peng_2014_RSC.Adv_4_62321
PubMedID:
Gene_locus related to this paper: biooc-ZHD101

Related information

Substrate Zearalenone
Gene_locus Zearalenone    biooc-ZHD101
Family Zearalenone    biooc-ZHD101    Zearalenone-hydrolase
Structure Zearalenone    biooc-ZHD101    Zearalenone-hydrolase    3WZL    3WZM

Citations formats

Peng W, Ko TP, Yang YY, Zheng YY, Chen CC, Zhu Z, Huang CH, Zeng YF, Huang JW, Wang AHJ, Liu JR, Guo RT (2014)
Crystal structure and substrate-binding mode of the mycoestrogen-detoxifying lactonase ZHD from Clonostachys rosea
RSC Advances 4 :62321

Peng W, Ko TP, Yang YY, Zheng YY, Chen CC, Zhu Z, Huang CH, Zeng YF, Huang JW, Wang AHJ, Liu JR, Guo RT (2014)
RSC Advances 4 :62321