The structure of a complex of the lactonohydrolase zearalenone hydrolase with the hydrolysis product of zearalenone at 1.60 Å resolution
| Autor: | Hong Lv, Kai Lei Sun, Wen Jing Yang, Xiao Jian Hu, Hu Jian Zhou, Qi Qi, Tian Yu Xu, Deng Ming Ming |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Models Molecular Protein Conformation alpha-Helical Resolution (mass spectrometry) Stereochemistry Hydrolases Recombinant Fusion Proteins Amino Acid Motifs Genetic Vectors Biophysics Gene Expression 010402 general chemistry Cleavage (embryo) Crystallography X-Ray 01 natural sciences Biochemistry Substrate Specificity Research Communications Fungal Proteins 03 medical and health sciences Hydrolysis chemistry.chemical_compound Structural Biology Hydrolase Genetics Escherichia coli Protein Interaction Domains and Motifs Cloning Molecular Mycotoxin Zearalenone chemistry.chemical_classification Binding Sites Chemistry zearalenone Condensed Matter Physics 0104 chemical sciences Kinetics 030104 developmental biology Enzyme Saccharomycetales Protein Conformation beta-Strand Clonostachys rosea lactonohydrolase Protein Multimerization catalysis mechansim Hydrophobic and Hydrophilic Interactions Lactone Protein Binding |
| Zdroj: | Acta Crystallographica. Section F, Structural Biology Communications |
| ISSN: | 2053-230X |
| Popis: | The high-resolution crystal structure of a complex of the lactonohydrolase zearalenone hydrolase with the hydrolytic product of the oestrogenic myotoxin zearalenone provides information on the final stage of the catalytic mechanism. 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 His6-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. |
| Databáze: | OpenAIRE |
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