ArticlePloS one2012
Crystal, solution and in silico structural studies of dihydrodipicolinate synthase from the common grapevine.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 40 citations in OpenAlex.
- A new lysine biosynthetic enzyme from a bacterial endosymbiont shaped by genetic drift and genome reduction.Protein science : a publication of the Protein Society · 2024Article
- ColorimetricHeliyon · 2023Article
- Engineering a feedback inhibition-insensitive plant dihydrodipicolinate synthase to increase lysine content in Camelina sativa seeds.Transgenic research · 2022Article
- An intact membrane is essential for small extracellular vesicle-induced modulation of α-synuclein fibrillization.Journal of extracellular vesicles · 2020Article
- Structure of the 4-hydroxy-tetrahydrodipicolinate synthase from the thermoacidophilic methanotroph Methylacidiphilum fumariolicum SolV and the phylogeny of the aminotransferase pathway.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Characterization of recombinant dihydrodipicolinate synthase from the bread wheat Triticum aestivum.Planta · 2018Article
- Molecular evolution of an oligomeric biocatalyst functioning in lysine biosynthesis.Biophysical reviews · 2018Review
- Structure and Function of Cyanobacterial DHDPS and DHDPR.Scientific reports · 2016Article
- Dimerization of Bacterial Diaminopimelate Decarboxylase Is Essential for Catalysis.The Journal of biological chemistry · 2016Article
- Genome-Wide Analysis of the Lysine Biosynthesis Pathway Network during Maize Seed Development.PloS one · 2016Article
- Cloning, expression, purification, crystallization and X-ray diffraction analysis of dihydrodipicolinate synthase from the human pathogenic bacterium Bartonella henselae strain Houston-1 at 2.1 Å resolution.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Crystal structure and in silico studies of dihydrodipicolinate synthase (DHDPS) from Aquifex aeolicus.Extremophiles : life under extreme conditions · 2014Article
- Evolutionary diversification of the multimeric states of proteins.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Structural, kinetic and computational investigation of Vitis vinifera DHDPS reveals new insight into the mechanism of lysine-mediated allosteric inhibition.Plant molecular biology · 2013Article
- Medicago truncatula dihydrodipicolinate synthase (DHDPS) enzymes display novel regulatory properties.Plant molecular biology · 2013Article
- From knock-out phenotype to three-dimensional structure of a promising antibiotic target from Streptococcus pneumoniae.PloS one · 2013Article
- Cloning, expression, purification and crystallization of dihydrodipicolinate synthase from Agrobacterium tumefaciens.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Characterisation of the first enzymes committed to lysine biosynthesis in Arabidopsis thaliana.PloS one · 2012Article
- Structural and dynamic requirements for optimal activity of the essential bacterial enzyme dihydrodipicolinate synthase.PLoS computational biology · 2012Article
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Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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