ArticleActa crystallographica. Section F, Structural biology and crystallization communications2008
Overexpression, purification, crystallization and preliminary X-ray analysis of Rv2780 from Mycobacterium tuberculosis H37Rv.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 7 citations in OpenAlex.
- Mycobacterium tuberculosis suppresses host antimicrobial peptides by dehydrogenating L-alanine.Nature communications · 2024Article
- Alanine dehydrogenases in mycobacteria.Journal of microbiology (Seoul, Korea) · 2019Review
- Salicylanilide diethyl phosphates as potential inhibitors of some mycobacterial enzymes.TheScientificWorldJournal · 2014Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
Rv2780, an alanine dehydrogenase from Mycobacterium tuberculosis (MtAlaDH), catalyzes the NAD-dependent interconversion of alanine and pyruvate. Alanine dehydrogenase is released into the culture medium in substantial amounts by virulent strains of mycobacteria and is not found in the vaccine strain of tuberculosis. Crystals of recombinant MtAlaDH were grown from 2 M ammonium sulfate solution at approximately 12 mg ml(-1) protein concentration in two crystal forms which occur in the presence and absence of NAD/pyruvate, respectively. Diffraction data extending to 2.6 A were collected at room temperature from both apo and ternary complex crystals. Crystals of the apoenzyme have unit-cell parameters a = 173.89, b = 127.07, c = 135.95 A. They are rod-like in shape and belong to space group C2. They contain a hexamer in the asymmetric unit. Crystals of the ternary complex belong to space group P4(3)2(1)2 and have unit-cell parameters a = b = 88.99, c = 373.85 A. There are three subunits in the asymmetric unit of the holoenzyme crystals.
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