ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
Cloning, expression and crystallization of dihydrodipicolinate reductase from methicillin-resistant Staphylococcus aureus.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Molecular evolution of an oligomeric biocatalyst functioning in lysine biosynthesis.Biophysical reviews · 2018Review
- The crystal structure of dihydrodipicolinate reductase from the human-pathogenic bacterium Bartonella henselae strain Houston-1 at 2.3 Å resolution.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Structure and Function of Cyanobacterial DHDPS and DHDPR.Scientific reports · 2016Article
- 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
- Cloning, expression, purification and crystallization of dihydrodipicolinate synthase from the grapevine Vitis vinifera.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Cloning, expression, purification and crystallization of dihydrodipicolinate synthase from the psychrophile Shewanella benthica.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dihydrodipicolinate reductase (DHDPR; EC 1.3.1.26) catalyzes the nucleotide (NADH/NADPH) dependent second step of the lysine-biosynthesis pathway in bacteria and plants. Here, the cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DHDPR from methicillin-resistant Staphylococcus aureus (MRSA-DHDPR) are presented. The enzyme was crystallized in a number of forms, predominantly with ammonium sulfate as a precipitant, with the best crystal form diffracting to beyond 3.65 A resolution. Crystal structures of the apo form as well as of cofactor (NADPH) bound and inhibitor (2,6-pyridinedicarboxylate) bound forms of MRSA-DHDPR will provide insight into the structure and function of this essential enzyme and valid drug target.
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