Structure reveals regulatory mechanisms of a MaoC-like hydratase from Phytophthora capsici involved in biosynthesis of polyhydroxyalkanoates (PHAs).

<h4>Background</h4>Polyhydroxyalkanoates (PHAs) have attracted increasing attention as "green plastic" due to their biodegradable, biocompatible, thermoplastic, and mechanical properties, and considerable research has been undertaken to develop low cost/high efficiency processe...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Huizheng Wang, Kai Zhang, Jie Zhu, Weiwei Song, Li Zhao, Xiuguo Zhang
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/0134070313e14613b5180ea686da2f63
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:0134070313e14613b5180ea686da2f63
record_format	dspace
spelling	oai:doaj.org-article:0134070313e14613b5180ea686da2f632021-11-18T08:47:21ZStructure reveals regulatory mechanisms of a MaoC-like hydratase from Phytophthora capsici involved in biosynthesis of polyhydroxyalkanoates (PHAs).1932-620310.1371/journal.pone.0080024https://doaj.org/article/0134070313e14613b5180ea686da2f632013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24244597/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>Polyhydroxyalkanoates (PHAs) have attracted increasing attention as "green plastic" due to their biodegradable, biocompatible, thermoplastic, and mechanical properties, and considerable research has been undertaken to develop low cost/high efficiency processes for the production of PHAs. MaoC-like hydratase (MaoC), which belongs to (R)-hydratase involved in linking the β-oxidation and the PHA biosynthetic pathways, has been identified recently. Understanding the regulatory mechanisms of (R)-hydratase catalysis is critical for efficient production of PHAs that promise synthesis an environment-friendly plastic.<h4>Methodology/principal findings</h4>We have determined the crystal structure of a new MaoC recognized from Phytophthora capsici. The crystal structure of the enzyme was solved at 2.00 Å resolution. The structure shows that MaoC has a canonical (R)-hydratase fold with an N-domain and a C-domain. Supporting its dimerization observed in structure, MaoC forms a stable homodimer in solution. Mutations that disrupt the dimeric MaoC result in a complete loss of activity toward crotonyl-CoA, indicating that dimerization is required for the enzymatic activity of MaoC. Importantly, structure comparison reveals that a loop unique to MaoC interacts with an α-helix that harbors the catalytic residues of MaoC. Deletion of the loop enhances the enzymatic activity of MaoC, suggesting its inhibitory role in regulating the activity of MaoC.<h4>Conclusions/significance</h4>The data in our study reveal the regulatory mechanism of an (R)-hydratase, providing information on enzyme engineering to produce low cost PHAs.Huizheng WangKai ZhangJie ZhuWeiwei SongLi ZhaoXiuguo ZhangPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 11, p e80024 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Huizheng Wang Kai Zhang Jie Zhu Weiwei Song Li Zhao Xiuguo Zhang Structure reveals regulatory mechanisms of a MaoC-like hydratase from Phytophthora capsici involved in biosynthesis of polyhydroxyalkanoates (PHAs).
description	<h4>Background</h4>Polyhydroxyalkanoates (PHAs) have attracted increasing attention as "green plastic" due to their biodegradable, biocompatible, thermoplastic, and mechanical properties, and considerable research has been undertaken to develop low cost/high efficiency processes for the production of PHAs. MaoC-like hydratase (MaoC), which belongs to (R)-hydratase involved in linking the β-oxidation and the PHA biosynthetic pathways, has been identified recently. Understanding the regulatory mechanisms of (R)-hydratase catalysis is critical for efficient production of PHAs that promise synthesis an environment-friendly plastic.<h4>Methodology/principal findings</h4>We have determined the crystal structure of a new MaoC recognized from Phytophthora capsici. The crystal structure of the enzyme was solved at 2.00 Å resolution. The structure shows that MaoC has a canonical (R)-hydratase fold with an N-domain and a C-domain. Supporting its dimerization observed in structure, MaoC forms a stable homodimer in solution. Mutations that disrupt the dimeric MaoC result in a complete loss of activity toward crotonyl-CoA, indicating that dimerization is required for the enzymatic activity of MaoC. Importantly, structure comparison reveals that a loop unique to MaoC interacts with an α-helix that harbors the catalytic residues of MaoC. Deletion of the loop enhances the enzymatic activity of MaoC, suggesting its inhibitory role in regulating the activity of MaoC.<h4>Conclusions/significance</h4>The data in our study reveal the regulatory mechanism of an (R)-hydratase, providing information on enzyme engineering to produce low cost PHAs.
format	article
author	Huizheng Wang Kai Zhang Jie Zhu Weiwei Song Li Zhao Xiuguo Zhang
author_facet	Huizheng Wang Kai Zhang Jie Zhu Weiwei Song Li Zhao Xiuguo Zhang
author_sort	Huizheng Wang
title	Structure reveals regulatory mechanisms of a MaoC-like hydratase from Phytophthora capsici involved in biosynthesis of polyhydroxyalkanoates (PHAs).
title_short	Structure reveals regulatory mechanisms of a MaoC-like hydratase from Phytophthora capsici involved in biosynthesis of polyhydroxyalkanoates (PHAs).
title_full	Structure reveals regulatory mechanisms of a MaoC-like hydratase from Phytophthora capsici involved in biosynthesis of polyhydroxyalkanoates (PHAs).
title_fullStr	Structure reveals regulatory mechanisms of a MaoC-like hydratase from Phytophthora capsici involved in biosynthesis of polyhydroxyalkanoates (PHAs).
title_full_unstemmed	Structure reveals regulatory mechanisms of a MaoC-like hydratase from Phytophthora capsici involved in biosynthesis of polyhydroxyalkanoates (PHAs).
title_sort	structure reveals regulatory mechanisms of a maoc-like hydratase from phytophthora capsici involved in biosynthesis of polyhydroxyalkanoates (phas).
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/0134070313e14613b5180ea686da2f63
work_keys_str_mv	AT huizhengwang structurerevealsregulatorymechanismsofamaoclikehydratasefromphytophthoracapsiciinvolvedinbiosynthesisofpolyhydroxyalkanoatesphas AT kaizhang structurerevealsregulatorymechanismsofamaoclikehydratasefromphytophthoracapsiciinvolvedinbiosynthesisofpolyhydroxyalkanoatesphas AT jiezhu structurerevealsregulatorymechanismsofamaoclikehydratasefromphytophthoracapsiciinvolvedinbiosynthesisofpolyhydroxyalkanoatesphas AT weiweisong structurerevealsregulatorymechanismsofamaoclikehydratasefromphytophthoracapsiciinvolvedinbiosynthesisofpolyhydroxyalkanoatesphas AT lizhao structurerevealsregulatorymechanismsofamaoclikehydratasefromphytophthoracapsiciinvolvedinbiosynthesisofpolyhydroxyalkanoatesphas AT xiuguozhang structurerevealsregulatorymechanismsofamaoclikehydratasefromphytophthoracapsiciinvolvedinbiosynthesisofpolyhydroxyalkanoatesphas
_version_	1718421302512975872

Structure reveals regulatory mechanisms of a MaoC-like hydratase from Phytophthora capsici involved in biosynthesis of polyhydroxyalkanoates (PHAs).

Ejemplares similares