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Structures of β-glycosidase LXYL-P1-2 reveals the product binding state of GH3 family and a specific pocket for Taxol recognition
LXYL-P1-2 is one of the few xylosidases that efficiently catalyze the reaction from 7-β-xylosyl-10-deacetyltaxol (XDT) to 10-deacetyltaxol (DT), and is a potential enzyme used in Taxol industrial production. Here we report the crystal structure of LXYL-P1-2 and its XDT binding complex. These structu...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6954215/ https://www.ncbi.nlm.nih.gov/pubmed/31925310 http://dx.doi.org/10.1038/s42003-019-0744-4 |
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author | Yang, Lin Chen, Tian-Jiao Wang, Fen Li, Li Yu, Wen-Bo Si, Yi-Kang Chen, Jing-Jing Liu, Wan-Cang Zhu, Ping Gong, Weimin |
author_facet | Yang, Lin Chen, Tian-Jiao Wang, Fen Li, Li Yu, Wen-Bo Si, Yi-Kang Chen, Jing-Jing Liu, Wan-Cang Zhu, Ping Gong, Weimin |
author_sort | Yang, Lin |
collection | PubMed |
description | LXYL-P1-2 is one of the few xylosidases that efficiently catalyze the reaction from 7-β-xylosyl-10-deacetyltaxol (XDT) to 10-deacetyltaxol (DT), and is a potential enzyme used in Taxol industrial production. Here we report the crystal structure of LXYL-P1-2 and its XDT binding complex. These structures reveal an enzyme/product complex with the sugar conformation different from the enzyme/substrate complex reported previously in GH3 enzymes, even in the whole glycohydrolases family. In addition, the DT binding pocket is identified as the structural basis for the substrate specificity. Further structure analysis reveals common features in LXYL-P1-2 and Taxol binding protein tubulin, which might provide useful information for designing new Taxol carrier proteins for drug delivery. |
format | Online Article Text |
id | pubmed-6954215 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-69542152020-01-13 Structures of β-glycosidase LXYL-P1-2 reveals the product binding state of GH3 family and a specific pocket for Taxol recognition Yang, Lin Chen, Tian-Jiao Wang, Fen Li, Li Yu, Wen-Bo Si, Yi-Kang Chen, Jing-Jing Liu, Wan-Cang Zhu, Ping Gong, Weimin Commun Biol Article LXYL-P1-2 is one of the few xylosidases that efficiently catalyze the reaction from 7-β-xylosyl-10-deacetyltaxol (XDT) to 10-deacetyltaxol (DT), and is a potential enzyme used in Taxol industrial production. Here we report the crystal structure of LXYL-P1-2 and its XDT binding complex. These structures reveal an enzyme/product complex with the sugar conformation different from the enzyme/substrate complex reported previously in GH3 enzymes, even in the whole glycohydrolases family. In addition, the DT binding pocket is identified as the structural basis for the substrate specificity. Further structure analysis reveals common features in LXYL-P1-2 and Taxol binding protein tubulin, which might provide useful information for designing new Taxol carrier proteins for drug delivery. Nature Publishing Group UK 2020-01-10 /pmc/articles/PMC6954215/ /pubmed/31925310 http://dx.doi.org/10.1038/s42003-019-0744-4 Text en © The Author(s) 2020 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 Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative 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 Yang, Lin Chen, Tian-Jiao Wang, Fen Li, Li Yu, Wen-Bo Si, Yi-Kang Chen, Jing-Jing Liu, Wan-Cang Zhu, Ping Gong, Weimin Structures of β-glycosidase LXYL-P1-2 reveals the product binding state of GH3 family and a specific pocket for Taxol recognition |
title | Structures of β-glycosidase LXYL-P1-2 reveals the product binding state of GH3 family and a specific pocket for Taxol recognition |
title_full | Structures of β-glycosidase LXYL-P1-2 reveals the product binding state of GH3 family and a specific pocket for Taxol recognition |
title_fullStr | Structures of β-glycosidase LXYL-P1-2 reveals the product binding state of GH3 family and a specific pocket for Taxol recognition |
title_full_unstemmed | Structures of β-glycosidase LXYL-P1-2 reveals the product binding state of GH3 family and a specific pocket for Taxol recognition |
title_short | Structures of β-glycosidase LXYL-P1-2 reveals the product binding state of GH3 family and a specific pocket for Taxol recognition |
title_sort | structures of β-glycosidase lxyl-p1-2 reveals the product binding state of gh3 family and a specific pocket for taxol recognition |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6954215/ https://www.ncbi.nlm.nih.gov/pubmed/31925310 http://dx.doi.org/10.1038/s42003-019-0744-4 |
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