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Crystal Structure and Potential Head-to-Middle Condensation Function of a Z,Z-Farnesyl Diphosphate Synthase
[Image: see text] Plants produce a wide variety of secondary metabolites in response to adverse environmental factors. Z,Z-Farnesyl diphosphate (Z,Z-FPP), synthesized by Z,Z-farnesyl diphosphate synthase (zFPS), supports the formation of phytochemicals in wild tomatoes. Here, the crystal structure o...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2017
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6044691/ https://www.ncbi.nlm.nih.gov/pubmed/30023621 http://dx.doi.org/10.1021/acsomega.6b00562 |
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author | Chan, Yueh-Te Ko, Tzu-Ping Yao, Shan-Hsueh Chen, Ya-Wen Lee, Cheng-Chung Wang, Andrew H.-J. |
author_facet | Chan, Yueh-Te Ko, Tzu-Ping Yao, Shan-Hsueh Chen, Ya-Wen Lee, Cheng-Chung Wang, Andrew H.-J. |
author_sort | Chan, Yueh-Te |
collection | PubMed |
description | [Image: see text] Plants produce a wide variety of secondary metabolites in response to adverse environmental factors. Z,Z-Farnesyl diphosphate (Z,Z-FPP), synthesized by Z,Z-farnesyl diphosphate synthase (zFPS), supports the formation of phytochemicals in wild tomatoes. Here, the crystal structure of N-terminal truncated zFPS (ΔzFPS) was determined. Irregular products including lavandulyl diphosphate and an unknown compound were surprisingly found. Apart from the truncated N-terminus as a functional regulator, structure-based analysis and mutagenesis assays revealed a residue H103 in ΔzFPS as one of the key elements to this irregular function. A series of substrate–enzyme complex structures were obtained from ΔzFPS-H103Y by co-crystallizing with isopentenyl diphosphate, dimethylallyl thiolodiphosphate, or both. Various substrate-binding modes were revealed. The catalytic mechanisms of both the head-to-tail and head-to-middle reactions in ΔzFPS were proposed. Functional switch between the two mechanisms in this enzyme and the essential role played by the flexible C-terminus were elucidated as well. |
format | Online Article Text |
id | pubmed-6044691 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-60446912018-07-16 Crystal Structure and Potential Head-to-Middle Condensation Function of a Z,Z-Farnesyl Diphosphate Synthase Chan, Yueh-Te Ko, Tzu-Ping Yao, Shan-Hsueh Chen, Ya-Wen Lee, Cheng-Chung Wang, Andrew H.-J. ACS Omega [Image: see text] Plants produce a wide variety of secondary metabolites in response to adverse environmental factors. Z,Z-Farnesyl diphosphate (Z,Z-FPP), synthesized by Z,Z-farnesyl diphosphate synthase (zFPS), supports the formation of phytochemicals in wild tomatoes. Here, the crystal structure of N-terminal truncated zFPS (ΔzFPS) was determined. Irregular products including lavandulyl diphosphate and an unknown compound were surprisingly found. Apart from the truncated N-terminus as a functional regulator, structure-based analysis and mutagenesis assays revealed a residue H103 in ΔzFPS as one of the key elements to this irregular function. A series of substrate–enzyme complex structures were obtained from ΔzFPS-H103Y by co-crystallizing with isopentenyl diphosphate, dimethylallyl thiolodiphosphate, or both. Various substrate-binding modes were revealed. The catalytic mechanisms of both the head-to-tail and head-to-middle reactions in ΔzFPS were proposed. Functional switch between the two mechanisms in this enzyme and the essential role played by the flexible C-terminus were elucidated as well. American Chemical Society 2017-03-16 /pmc/articles/PMC6044691/ /pubmed/30023621 http://dx.doi.org/10.1021/acsomega.6b00562 Text en Copyright © 2017 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes. |
spellingShingle | Chan, Yueh-Te Ko, Tzu-Ping Yao, Shan-Hsueh Chen, Ya-Wen Lee, Cheng-Chung Wang, Andrew H.-J. Crystal Structure and Potential Head-to-Middle Condensation Function of a Z,Z-Farnesyl Diphosphate Synthase |
title | Crystal Structure and Potential Head-to-Middle Condensation
Function of a Z,Z-Farnesyl Diphosphate Synthase |
title_full | Crystal Structure and Potential Head-to-Middle Condensation
Function of a Z,Z-Farnesyl Diphosphate Synthase |
title_fullStr | Crystal Structure and Potential Head-to-Middle Condensation
Function of a Z,Z-Farnesyl Diphosphate Synthase |
title_full_unstemmed | Crystal Structure and Potential Head-to-Middle Condensation
Function of a Z,Z-Farnesyl Diphosphate Synthase |
title_short | Crystal Structure and Potential Head-to-Middle Condensation
Function of a Z,Z-Farnesyl Diphosphate Synthase |
title_sort | crystal structure and potential head-to-middle condensation
function of a z,z-farnesyl diphosphate synthase |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6044691/ https://www.ncbi.nlm.nih.gov/pubmed/30023621 http://dx.doi.org/10.1021/acsomega.6b00562 |
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