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Chloramphenicol phosphotransferase-like protein family

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Chloramphenicol phosphotransferase-like protein
crystal structure of atu3015, a putative cytidylate kinase from agrobacterium tumefaciens, northeast structural genomics target atr62
Identifiers
SymbolCPT
PfamPF07931
Pfam clanCL0023
InterProIPR012853
SCOP21grq / SCOPe / SUPFAM
CDDcd00227
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

In molecular biology, the chloramphenicol phosphotransferase-like protein family includes the chloramphenicol 3-O phosphotransferase (CPT) expressed by Streptomyces venezuelae. Chloramphenicol (Cm) is a metabolite produced by this bacterium that can inhibit ribosomal peptidyl transferase activity and therefore protein production. By transferring a phosphate group to the C-3 hydroxyl group of Cm, CPT inactivates this potentially lethal metabolite.[1][2]

References

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  1. ^ Izard T (August 2001). "Structural basis for chloramphenicol tolerance in Streptomyces venezuelae by chloramphenicol phosphotransferase activity". Protein Science. 10 (8): 1508–13. doi:10.1002/pro.101508. PMC 2374082. PMID 11468347.
  2. ^ Izard T, Ellis J (June 2000). "The crystal structures of chloramphenicol phosphotransferase reveal a novel inactivation mechanism". The EMBO Journal. 19 (11): 2690–700. doi:10.1093/emboj/19.11.2690. PMC 212772. PMID 10835366.
This article incorporates text from the public domain Pfam and InterPro: IPR012853