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A structural characterization of the isoniazid Mycobacterium tuberculosis drug target, Rv2971, in its unliganded form.

Shahine A, Prasetyoputri A, Rossjohn J, Beddoe T
Acta Crystallogr F Struct Biol Commun 70 572-7 (2014)
Cited: 3 times
EuropePMC logo PMID: 24817712

Abstract

Aldo-keto reductases (AKR) are a large superfamily of NADPH-dependent oxidoreductases and play a role in detoxification of toxic metabolites. Rv2971, an AKR in Mycobacterium tuberculosis, has recently been identified as a target of isoniazid, a key first-line drug against tuberculosis. Here, the cloning, expression, purification, crystallization and structural characterization of Rv2971 are described. To gain insight into its function, the crystal structure of Rv2971 was successfully determined to 1.60 Å resolution in its unliganded form. The structure exhibits a TIM-barrel fold typical of AKRs, revealing structural characteristics essential for function and substrate specificities, allowing a structural comparison between Rv2971 and other mycobacterial AKRs.

Articles - 4otk mentioned but not cited (2)

  1. A structural characterization of the isoniazid Mycobacterium tuberculosis drug target, Rv2971, in its unliganded form. Shahine A, Prasetyoputri A, Rossjohn J, Beddoe T. Acta Crystallogr F Struct Biol Commun 70 572-577 (2014)
  2. In silico analysis to identify potential antitubercular molecules in Morus alba through virtual screening and molecular dynamics simulations. Khan M, Khan S, Alshammary FL, Zaidi S, Singh V, Ahmad I, Patel H, Gupta VK, Haque S. J Biomol Struct Dyn 1-8 (2023)


Articles citing this publication (1)

  1. Using a Label Free Quantitative Proteomics Approach to Identify Changes in Protein Abundance in Multidrug-Resistant Mycobacterium tuberculosis. Phong TQ, Ha do TT, Volker U, Hammer E. Indian J Microbiol 55 219-230 (2015)


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