Crystal, solution and in silico structural studies of dihydrodipicolinate synthase from the common grapevine.

Dihydrodipicolinate synthase (DHDPS) catalyzes the rate limiting step in lysine biosynthesis in bacteria and plants. The structure of DHDPS has been determined from several bacterial species and shown in most cases to form a homotetramer or dimer of dimers. However, only one plant DHDPS structure ha...

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Autores principales:	Sarah C Atkinson, Con Dogovski, Matthew T Downton, F Grant Pearce, Cyril F Reboul, Ashley M Buckle, Juliet A Gerrard, Renwick C J Dobson, John Wagner, Matthew A Perugini
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/fd29a4c895724e209e09c54f98419d8e
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spelling	oai:doaj.org-article:fd29a4c895724e209e09c54f98419d8e2021-11-18T07:14:30ZCrystal, solution and in silico structural studies of dihydrodipicolinate synthase from the common grapevine.1932-620310.1371/journal.pone.0038318https://doaj.org/article/fd29a4c895724e209e09c54f98419d8e2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22761676/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Dihydrodipicolinate synthase (DHDPS) catalyzes the rate limiting step in lysine biosynthesis in bacteria and plants. The structure of DHDPS has been determined from several bacterial species and shown in most cases to form a homotetramer or dimer of dimers. However, only one plant DHDPS structure has been determined to date from the wild tobacco species, Nicotiana sylvestris (Blickling et al. (1997) J. Mol. Biol. 274, 608-621). Whilst N. sylvestris DHDPS also forms a homotetramer, the plant enzyme adopts a 'back-to-back' dimer of dimers compared to the 'head-to-head' architecture observed for bacterial DHDPS tetramers. This raises the question of whether the alternative quaternary architecture observed for N. sylvestris DHDPS is common to all plant DHDPS enzymes. Here, we describe the structure of DHDPS from the grapevine plant, Vitis vinifera, and show using analytical ultracentrifugation, small-angle X-ray scattering and X-ray crystallography that V. vinifera DHDPS forms a 'back-to-back' homotetramer, consistent with N. sylvestris DHDPS. This study is the first to demonstrate using both crystal and solution state measurements that DHDPS from the grapevine plant adopts an alternative tetrameric architecture to the bacterial form, which is important for optimizing protein dynamics as suggested by molecular dynamics simulations reported in this study.Sarah C AtkinsonCon DogovskiMatthew T DowntonF Grant PearceCyril F ReboulAshley M BuckleJuliet A GerrardRenwick C J DobsonJohn WagnerMatthew A PeruginiPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 6, p e38318 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Sarah C Atkinson Con Dogovski Matthew T Downton F Grant Pearce Cyril F Reboul Ashley M Buckle Juliet A Gerrard Renwick C J Dobson John Wagner Matthew A Perugini Crystal, solution and in silico structural studies of dihydrodipicolinate synthase from the common grapevine.
description	Dihydrodipicolinate synthase (DHDPS) catalyzes the rate limiting step in lysine biosynthesis in bacteria and plants. The structure of DHDPS has been determined from several bacterial species and shown in most cases to form a homotetramer or dimer of dimers. However, only one plant DHDPS structure has been determined to date from the wild tobacco species, Nicotiana sylvestris (Blickling et al. (1997) J. Mol. Biol. 274, 608-621). Whilst N. sylvestris DHDPS also forms a homotetramer, the plant enzyme adopts a 'back-to-back' dimer of dimers compared to the 'head-to-head' architecture observed for bacterial DHDPS tetramers. This raises the question of whether the alternative quaternary architecture observed for N. sylvestris DHDPS is common to all plant DHDPS enzymes. Here, we describe the structure of DHDPS from the grapevine plant, Vitis vinifera, and show using analytical ultracentrifugation, small-angle X-ray scattering and X-ray crystallography that V. vinifera DHDPS forms a 'back-to-back' homotetramer, consistent with N. sylvestris DHDPS. This study is the first to demonstrate using both crystal and solution state measurements that DHDPS from the grapevine plant adopts an alternative tetrameric architecture to the bacterial form, which is important for optimizing protein dynamics as suggested by molecular dynamics simulations reported in this study.
format	article
author	Sarah C Atkinson Con Dogovski Matthew T Downton F Grant Pearce Cyril F Reboul Ashley M Buckle Juliet A Gerrard Renwick C J Dobson John Wagner Matthew A Perugini
author_facet	Sarah C Atkinson Con Dogovski Matthew T Downton F Grant Pearce Cyril F Reboul Ashley M Buckle Juliet A Gerrard Renwick C J Dobson John Wagner Matthew A Perugini
author_sort	Sarah C Atkinson
title	Crystal, solution and in silico structural studies of dihydrodipicolinate synthase from the common grapevine.
title_short	Crystal, solution and in silico structural studies of dihydrodipicolinate synthase from the common grapevine.
title_full	Crystal, solution and in silico structural studies of dihydrodipicolinate synthase from the common grapevine.
title_fullStr	Crystal, solution and in silico structural studies of dihydrodipicolinate synthase from the common grapevine.
title_full_unstemmed	Crystal, solution and in silico structural studies of dihydrodipicolinate synthase from the common grapevine.
title_sort	crystal, solution and in silico structural studies of dihydrodipicolinate synthase from the common grapevine.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/fd29a4c895724e209e09c54f98419d8e
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Crystal, solution and in silico structural studies of dihydrodipicolinate synthase from the common grapevine.

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