spacer
spacer

PDBsum entry 2wyu

Go to PDB code: 
protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
2wyu
Jmol
Contents
Protein chains
256 a.a. *
Ligands
GOL ×2
Metals
_NA ×3
Waters ×1064
* Residue conservation analysis
PDB id:
2wyu
Name: Oxidoreductase
Title: High resolution structure of thermus thermophilus enoyl- acyl carrier protein reductase apo-form
Structure: Enoyl-[acyl carrier protein] reductase. Chain: a, b, c, d. Engineered: yes
Source: Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Atcc: 27634. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_variant: de3. Other_details: thermus thermophilus DNA obtained from prof. Wolfgang liebl, goettingen.
Resolution:
1.50Å     R-factor:   0.170     R-free:   0.199
Authors: J.M.Otero,A.J.Noel,P.Guardado-Calvo,A.L.Llamas-Saiz,M.J.Van
Key ref: J.M.Otero et al. (2012). High-resolution structures of Thermus thermophilus enoyl-acyl carrier protein reductase in the apo form, in complex with NAD+ and in complex with NAD+ and triclosan. Acta Crystallogr Sect F Struct Biol Cryst Commun, 68, 1139-1148. PubMed id: 23027736 DOI: 10.1107/S1744309112033982
Date:
20-Nov-09     Release date:   24-Nov-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q5SLI9  (Q5SLI9_THET8) -  Enoyl-[acyl-carrier-protein] reductase [NADH]
Seq:
Struc:
261 a.a.
256 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.3.1.9  - 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 = GOL)
matches with 44.44% similarity
+ NAD(+)
= trans-2,3-dehydroacyl-[acyl- carrier protein]
+ NADH
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   3 terms 
  Biochemical function     nucleotide binding     3 terms  

 

 
    reference    
 
 
DOI no: 10.1107/S1744309112033982 Acta Crystallogr Sect F Struct Biol Cryst Commun 68:1139-1148 (2012)
PubMed id: 23027736  
 
 
High-resolution structures of Thermus thermophilus enoyl-acyl carrier protein reductase in the apo form, in complex with NAD+ and in complex with NAD+ and triclosan.
J.M.Otero, A.J.Noël, P.Guardado-Calvo, A.L.Llamas-Saiz, W.Wende, B.Schierling, A.Pingoud, M.J.van Raaij.
 
  ABSTRACT  
 
Enoyl-acyl carrier protein reductase (ENR; the product of the fabI gene) is an important enzyme that is involved in the type II fatty-acid-synthesis pathway of bacteria, plants, apicomplexan protozoa and mitochondria. Harmful pathogens such as Mycobacterium tuberculosis and Plasmodium falciparum use the type II fatty-acid-synthesis system, but not mammals or fungi, which contain a type I fatty-acid-synthesis pathway consisting of one or two multifunctional enzymes. For this reason, specific inhibitors of ENR are attractive antibiotic candidates. Triclosan, a broad-range antibacterial agent, binds to ENR, inhibiting fatty-acid synthesis. As humans do not have an ENR enzyme, they are not affected. Here, high-resolution structures of Thermus thermophilus (Tth) ENR in the apo form, bound to NAD(+) and bound to NAD(+) plus triclosan are reported. Differences from and similarities to other known ENR structures are reported; in general, the structures are very similar. The cofactor-binding site is also very similar to those of other ENRs and, as reported for other species, triclosan leads to greater ordering of the loop that covers the cofactor-binding site, which, together with the presence of triclosan itself, presumably provides tight binding of the dinucleotide, preventing cycling of the cofactor. Differences between the structures of Tth ENR and other ENRs are the presence of an additional β-sheet at the N-terminus and a larger number of salt bridges and side-chain hydrogen bonds. These features may be related to the high thermal stability of Tth ENR.