2NTN

Crystal structure of MabA-C60V/G139A/S144L


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.238 
  • R-Value Work: 0.177 
  • R-Value Observed: 0.181 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Lack of dynamics in the MabA active site kills the enzyme activity: practical consequences for drug-design studies

Poncet-Montange, G.Ducasse-Cabanot, S.Quemard, A.Labesse, G.Cohen-Gonsaud, M.

(2007) Acta Crystallogr D Biol Crystallogr 63: 923-925

  • DOI: https://doi.org/10.1107/S0907444907024158
  • Primary Citation of Related Structures:  
    2NTN

  • PubMed Abstract: 

    The MabA protein from Mycobacterium tuberculosis is a validated drug target. Previous structural studies of this protein showed dynamic behaviour in the catalytic site and described motion between an open 'active' holo form (with NADP) and a closed 'inactive' apo form (without NADP). Here, a mutation (G139A) is reported that leads to complete protein inactivation and freezes the catalytic site into its closed form, even in the presence of the cofactor. This observation suggests a new way to develop anti-MabA drugs via protein stabilization of the 'inactive' form.


  • Organizational Affiliation

    CNRS UMR5048, Centre de Biochimie Structurale, F-34090 Montpellier, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
3-oxoacyl-[acyl-carrier-protein] reductase
A, B
267Mycobacterium tuberculosis H37RvMutation(s): 3 
Gene Names: fabGfabG1
EC: 1.1.1.100
UniProt
Find proteins for P9WGT3 (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
Explore P9WGT3 
Go to UniProtKB:  P9WGT3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP9WGT3
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.238 
  • R-Value Work: 0.177 
  • R-Value Observed: 0.181 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 81.613α = 90
b = 117.285β = 121.9
c = 52.272γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
CCP4data scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-11-21
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Derived calculations, Version format compliance
  • Version 1.3: 2021-11-10
    Changes: Database references
  • Version 1.4: 2023-10-25
    Changes: Data collection, Refinement description