PDBsum entry 3nrc

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protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
Protein chains
256 a.a. *
NAD ×2
TCL ×2
Waters ×142
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: Crystal stucture of the francisella tularensis enoyl-acyl ca protein reductase (fabi) in complex with NAD+ and triclosan
Structure: Enoyl-[acyl-carrier-protein] reductase (nadh). Chain: a, b. Engineered: yes
Source: Francisella tularensis subsp. Tularens organism_taxid: 177416. Strain: schu4. Gene: fabi, fabi gene, ftt_0782. Expressed in: escherichia coli. Expression_system_taxid: 469008.
2.10Å     R-factor:   0.189     R-free:   0.242
Authors: S.Mehboob,B.D.Santarsiero,K.Truong,M.E.Johnson
Key ref: S.Mehboob et al. (2010). Structure of the Francisella tularensis enoyl-acyl carrier protein reductase (FabI) in complex with NAD(+) and triclosan. Acta Crystallogr Sect F Struct Biol Cryst Commun, 66, 1436-1440. PubMed id: 21045289
30-Jun-10     Release date:   10-Nov-10    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q5NGQ3  (Q5NGQ3_FRATT) -  Enoyl-[acyl-carrier-protein] reductase [NADH]
260 a.a.
256 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Enoyl-[acyl-carrier-protein] reductase (NADH).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: An acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl- carrier protein] + NADH
acyl-[acyl-carrier protein]
Bound ligand (Het Group name = NAD)
corresponds exactly
= trans-2,3-dehydroacyl-[acyl- carrier protein]
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   2 terms 
  Biochemical function     nucleotide binding     3 terms  


Acta Crystallogr Sect F Struct Biol Cryst Commun 66:1436-1440 (2010)
PubMed id: 21045289  
Structure of the Francisella tularensis enoyl-acyl carrier protein reductase (FabI) in complex with NAD(+) and triclosan.
S.Mehboob, K.Truong, B.D.Santarsiero, M.E.Johnson.
Enoyl-acyl carrier protein reductase (FabI) catalyzes the last rate-limiting step in the elongation cycle of the fatty-acid biosynthesis pathway and has been validated as a potential antimicrobial drug target in Francisella tularensis. The development of new antibiotic therapies is important both to combat potential drug-resistant bioweapons and to address the broader societal problem of increasing antibiotic resistance among many pathogenic bacteria. The crystal structure of FabI from F. tularensis (FtuFabI) in complex with the inhibitor triclosan and the cofactor NAD(+) has been solved to a resolution of 2.1 Å. Triclosan is known to effectively inhibit FabI from different organisms. Precise characterization of the mode of triclosan binding is required to develop highly specific inhibitors. Comparison of our structure with the previously determined FtuFabI structure (PDB code 2jjy) which is bound to only NAD(+) reveals the conformation of the substrate-binding loop, electron density for which was missing in the earlier structure, and demonstrates a shift in the conformation of the NAD(+) cofactor. This shift in the position of the phosphate groups allows more room in the active site for substrate or inhibitor to bind and be better accommodated. This information will be crucial for virtual screening studies to identify novel scaffolds for development into new active inhibitors.