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PDBsum entry 2ntn

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protein Protein-protein interface(s) links
Oxidoreductase PDB id
2ntn
Jmol
Contents
Protein chains
218 a.a. *
207 a.a. *
Waters ×239
* Residue conservation analysis
PDB id:
2ntn
Name: Oxidoreductase
Title: Crystal structure of maba-c60v/g139a/s144l
Structure: 3-oxoacyl-[acyl-carrier-protein] reductase. Chain: a, b. Synonym: 3-ketoacyl-acyl carrier protein reductase, beta-ke carrier protein reductase. Engineered: yes. Mutation: yes
Source: Mycobacterium tuberculosis h37rv. Organism_taxid: 83332. Strain: h37rv. Gene: fabg, fabg1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Dimer (from PDB file)
Resolution:
2.30Å     R-factor:   0.181     R-free:   0.238
Authors: G.Poncet-Montange,S.Ducasse-Cabanot,A.Quemard,G.Labesse,M.Co Gonsaud
Key ref:
G.Poncet-Montange et al. (2007). Lack of dynamics in the MabA active site kills the enzyme activity: practical consequences for drug-design studies. Acta Crystallogr D Biol Crystallogr, 63, 923-925. PubMed id: 17642518 DOI: 10.1107/S0907444907024158
Date:
08-Nov-06     Release date:   21-Nov-06    
PROCHECK
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 Headers
 References

Protein chain
Pfam  
P9WGT3  (FABG_MYCTU) -  3-oxoacyl-[acyl-carrier-protein] reductase FabG1
Seq:
Struc:
247 a.a.
218 a.a.*
Protein chain
Pfam  
P9WGT3  (FABG_MYCTU) -  3-oxoacyl-[acyl-carrier-protein] reductase FabG1
Seq:
Struc:
247 a.a.
207 a.a.*
Key:    Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.1.1.1.100  - 3-oxoacyl-[acyl-carrier-protein] reductase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl- carrier-protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier-protein]
+ NADP(+)
= 3-oxoacyl-[acyl- carrier-protein]
+ NADPH
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     plasma membrane   1 term 
  Biological process     metabolic process   5 terms 
  Biochemical function     oxidoreductase activity     2 terms  

 

 
    reference    
 
 
DOI no: 10.1107/S0907444907024158 Acta Crystallogr D Biol Crystallogr 63:923-925 (2007)
PubMed id: 17642518  
 
 
Lack of dynamics in the MabA active site kills the enzyme activity: practical consequences for drug-design studies.
G.Poncet-Montange, S.Ducasse-Cabanot, A.Quemard, G.Labesse, M.Cohen-Gonsaud.
 
  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.
 
  Selected figure(s)  
 
Figure 1.
Figure 1 Superposition of the closed inactive form (in light blue) and the open active form (in dark blue). The catalytic Ser140 and Tyr153 are shown in stick representation. The rearranged regions of the protein are represented in yellow for the open form and orange for the closed form. Residue 139 is coloured red.
 
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2007, 63, 923-925) copyright 2007.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21081168 D.Dutta, S.Bhattacharyya, S.Mukherjee, B.Saha, and A.K.Das (2011).
Crystal structure of FabG4 from Mycobacterium tuberculosis reveals the importance of C-terminal residues in ketoreductase activity.
  J Struct Biol, 174, 147-155.
PDB code: 3m1l
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