Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Chan, Yueh-Te, Ko, Tzu-Ping, Yao, Shan-Hsueh, Chen, Ya-Wen, Lee, Cheng-Chung, Wang, Andrew H.-J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2017
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
_version_ 1783339522478571520
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
work_keys_str_mv AT chanyuehte crystalstructureandpotentialheadtomiddlecondensationfunctionofazzfarnesyldiphosphatesynthase
AT kotzuping crystalstructureandpotentialheadtomiddlecondensationfunctionofazzfarnesyldiphosphatesynthase
AT yaoshanhsueh crystalstructureandpotentialheadtomiddlecondensationfunctionofazzfarnesyldiphosphatesynthase
AT chenyawen crystalstructureandpotentialheadtomiddlecondensationfunctionofazzfarnesyldiphosphatesynthase
AT leechengchung crystalstructureandpotentialheadtomiddlecondensationfunctionofazzfarnesyldiphosphatesynthase
AT wangandrewhj crystalstructureandpotentialheadtomiddlecondensationfunctionofazzfarnesyldiphosphatesynthase