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The structure of a complex of the lactonohydrolase zearalenone hydrolase with the hydrolysis product of zearalenone at 1.60 Å resolution

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, th...

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Autores principales: Qi, Qi, Yang, Wen-Jing, Zhou, Hu-Jian, Ming, Deng-Ming, Sun, Kai-Lei, Xu, Tian-Yu, Hu, Xiao-Jian, Lv, Hong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5505240/
https://www.ncbi.nlm.nih.gov/pubmed/28695844
http://dx.doi.org/10.1107/S2053230X17007713
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author Qi, Qi
Yang, Wen-Jing
Zhou, Hu-Jian
Ming, Deng-Ming
Sun, Kai-Lei
Xu, Tian-Yu
Hu, Xiao-Jian
Lv, Hong
author_facet Qi, Qi
Yang, Wen-Jing
Zhou, Hu-Jian
Ming, Deng-Ming
Sun, Kai-Lei
Xu, Tian-Yu
Hu, Xiao-Jian
Lv, Hong
author_sort Qi, Qi
collection PubMed
description 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(6)-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(∊1), 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.
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spelling pubmed-55052402017-07-31 The structure of a complex of the lactonohydrolase zearalenone hydrolase with the hydrolysis product of zearalenone at 1.60 Å resolution Qi, Qi Yang, Wen-Jing Zhou, Hu-Jian Ming, Deng-Ming Sun, Kai-Lei Xu, Tian-Yu Hu, Xiao-Jian Lv, Hong Acta Crystallogr F Struct Biol Commun Research Communications 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(6)-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(∊1), 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. International Union of Crystallography 2017-06-17 /pmc/articles/PMC5505240/ /pubmed/28695844 http://dx.doi.org/10.1107/S2053230X17007713 Text en © Qi et al. 2017 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/2.0/uk/
spellingShingle Research Communications
Qi, Qi
Yang, Wen-Jing
Zhou, Hu-Jian
Ming, Deng-Ming
Sun, Kai-Lei
Xu, Tian-Yu
Hu, Xiao-Jian
Lv, Hong
The structure of a complex of the lactonohydrolase zearalenone hydrolase with the hydrolysis product of zearalenone at 1.60 Å resolution
title The structure of a complex of the lactonohydrolase zearalenone hydrolase with the hydrolysis product of zearalenone at 1.60 Å resolution
title_full The structure of a complex of the lactonohydrolase zearalenone hydrolase with the hydrolysis product of zearalenone at 1.60 Å resolution
title_fullStr The structure of a complex of the lactonohydrolase zearalenone hydrolase with the hydrolysis product of zearalenone at 1.60 Å resolution
title_full_unstemmed The structure of a complex of the lactonohydrolase zearalenone hydrolase with the hydrolysis product of zearalenone at 1.60 Å resolution
title_short The structure of a complex of the lactonohydrolase zearalenone hydrolase with the hydrolysis product of zearalenone at 1.60 Å resolution
title_sort structure of a complex of the lactonohydrolase zearalenone hydrolase with the hydrolysis product of zearalenone at 1.60 å resolution
topic Research Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5505240/
https://www.ncbi.nlm.nih.gov/pubmed/28695844
http://dx.doi.org/10.1107/S2053230X17007713
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