4OTK

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


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.169 
  • R-Value Work: 0.146 
  • R-Value Observed: 0.147 

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This is version 1.4 of the entry. See complete history


Literature

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

Shahine, A.Prasetyoputri, A.Rossjohn, J.Beddoe, T.

(2014) Acta Crystallogr Sect F Struct Biol Cryst Commun 70: 572-577

  • DOI: https://doi.org/10.1107/S2053230X14007158
  • Primary Citation of Related Structures:  
    4OTK

  • PubMed 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.


  • Organizational Affiliation

    Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, Australia.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Mycobacterial Enzyme Rv2971318Mycobacterium tuberculosisMutation(s): 0 
Gene Names: Rv2971MT3049
EC: 1
UniProt
Find proteins for P9WQA5 (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
Explore P9WQA5 
Go to UniProtKB:  P9WQA5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP9WQA5
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.169 
  • R-Value Work: 0.146 
  • R-Value Observed: 0.147 
  • Space Group: P 32 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 86.27α = 90
b = 86.27β = 90
c = 86.29γ = 120
Software Package:
Software NamePurpose
ADSCdata collection
PHENIXrefinement
MOSFLMdata reduction
SCALAdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-05-07
    Type: Initial release
  • Version 1.1: 2014-05-14
    Changes: Database references
  • Version 1.2: 2014-06-04
    Changes: Database references
  • Version 1.3: 2017-11-22
    Changes: Refinement description, Structure summary
  • Version 1.4: 2023-11-08
    Changes: Data collection, Database references, Derived calculations, Refinement description