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PDBsum entry 4mjq

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protein ligands metals Protein-protein interface(s) links
Transferase/transferase inhibitor PDB id
4mjq
Jmol
Contents
Protein chains
362 a.a.
Ligands
27R
PGE ×2
EDO
PG4
Metals
_CL ×2
_CA ×3
Waters ×651
PDB id:
4mjq
Name: Transferase/transferase inhibitor
Title: E. Coli sliding clamp in complex with bromfenac
Structure: DNA polymerase iii subunit beta. Chain: a, b. Synonym: beta sliding clamp, beta clamp. Engineered: yes
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: b3701, dnan, jw3678. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.73Å     R-factor:   0.187     R-free:   0.218
Authors: Z.Yin,A.J.Oakley
Key ref: Z.Yin et al. (2014). DNA replication is the target for the antibacterial effects of nonsteroidal anti-inflammatory drugs. Chem Biol, 21, 481-487. PubMed id: 24631121 DOI: 10.1016/j.chembiol.2014.02.009
Date:
04-Sep-13     Release date:   18-Sep-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0A988  (DPO3B_ECOLI) -  DNA polymerase III subunit beta
Seq:
Struc:
366 a.a.
362 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.7.7  - DNA-directed Dna polymerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Deoxynucleoside triphosphate
+ DNA(n)
= diphosphate
+ DNA(n+1)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   3 terms 
  Biological process     DNA biosynthetic process   5 terms 
  Biochemical function     protein binding     7 terms  

 

 
    reference    
 
 
DOI no: 10.1016/j.chembiol.2014.02.009 Chem Biol 21:481-487 (2014)
PubMed id: 24631121  
 
 
DNA replication is the target for the antibacterial effects of nonsteroidal anti-inflammatory drugs.
Z.Yin, Y.Wang, L.R.Whittell, S.Jergic, M.Liu, E.Harry, N.E.Dixon, M.J.Kelso, J.L.Beck, A.J.Oakley.
 
  ABSTRACT  
 
Evidence suggests that some nonsteroidal anti-inflammatory drugs (NSAIDs) possess antibacterial properties with an unknown mechanism. We describe the in vitro antibacterial properties of the NSAIDs carprofen, bromfenac, and vedaprofen, and show that these NSAIDs inhibit the Escherichia coli DNA polymerase III β subunit, an essential interaction hub that acts as a mobile tether on DNA for many essential partner proteins in DNA replication and repair. Crystal structures show that the three NSAIDs bind to the sliding clamp at a common binding site required for partner binding. Inhibition of interaction of the clamp loader and/or the replicative polymerase α subunit with the sliding clamp is demonstrated using an in vitro DNA replication assay. NSAIDs thus present promising lead scaffolds for novel antibacterial agents targeting the sliding clamp.