Structural insight into catalytic mechanism of PET hydrolase

PET hydrolase (PETase), which hydrolyzes polyethylene terephthalate (PET) into soluble building blocks, provides an attractive avenue for the bioconversion of plastics. Here we present the structures of a novel PETase from the PET-consuming microbe Ideonella sakaiensis in complex with substrate and...

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Autores principales: Han, Xu, Liu, Weidong, Huang, Jian-Wen, Ma, Jiantao, Zheng, Yingying, Ko, Tzu-Ping, Xu, Limin, Cheng, Ya-Shan, Chen, Chun-Chi, Guo, Rey-Ting
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5727383/
https://www.ncbi.nlm.nih.gov/pubmed/29235460
http://dx.doi.org/10.1038/s41467-017-02255-z
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author Han, Xu
Liu, Weidong
Huang, Jian-Wen
Ma, Jiantao
Zheng, Yingying
Ko, Tzu-Ping
Xu, Limin
Cheng, Ya-Shan
Chen, Chun-Chi
Guo, Rey-Ting
author_facet Han, Xu
Liu, Weidong
Huang, Jian-Wen
Ma, Jiantao
Zheng, Yingying
Ko, Tzu-Ping
Xu, Limin
Cheng, Ya-Shan
Chen, Chun-Chi
Guo, Rey-Ting
author_sort Han, Xu
collection PubMed
description PET hydrolase (PETase), which hydrolyzes polyethylene terephthalate (PET) into soluble building blocks, provides an attractive avenue for the bioconversion of plastics. Here we present the structures of a novel PETase from the PET-consuming microbe Ideonella sakaiensis in complex with substrate and product analogs. Through structural analyses, mutagenesis, and activity measurements, a substrate-binding mode is proposed, and several features critical for catalysis are elucidated.
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spelling pubmed-57273832017-12-14 Structural insight into catalytic mechanism of PET hydrolase Han, Xu Liu, Weidong Huang, Jian-Wen Ma, Jiantao Zheng, Yingying Ko, Tzu-Ping Xu, Limin Cheng, Ya-Shan Chen, Chun-Chi Guo, Rey-Ting Nat Commun Article PET hydrolase (PETase), which hydrolyzes polyethylene terephthalate (PET) into soluble building blocks, provides an attractive avenue for the bioconversion of plastics. Here we present the structures of a novel PETase from the PET-consuming microbe Ideonella sakaiensis in complex with substrate and product analogs. Through structural analyses, mutagenesis, and activity measurements, a substrate-binding mode is proposed, and several features critical for catalysis are elucidated. Nature Publishing Group UK 2017-12-13 /pmc/articles/PMC5727383/ /pubmed/29235460 http://dx.doi.org/10.1038/s41467-017-02255-z Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commonslicense, unless indicated otherwise in a credit line to the material. If material is not included in the article’sCreative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Han, Xu
Liu, Weidong
Huang, Jian-Wen
Ma, Jiantao
Zheng, Yingying
Ko, Tzu-Ping
Xu, Limin
Cheng, Ya-Shan
Chen, Chun-Chi
Guo, Rey-Ting
Structural insight into catalytic mechanism of PET hydrolase
title Structural insight into catalytic mechanism of PET hydrolase
title_full Structural insight into catalytic mechanism of PET hydrolase
title_fullStr Structural insight into catalytic mechanism of PET hydrolase
title_full_unstemmed Structural insight into catalytic mechanism of PET hydrolase
title_short Structural insight into catalytic mechanism of PET hydrolase
title_sort structural insight into catalytic mechanism of pet hydrolase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5727383/
https://www.ncbi.nlm.nih.gov/pubmed/29235460
http://dx.doi.org/10.1038/s41467-017-02255-z
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