Chloramphenicol phosphotransferase-like protein family

Chloramphenicol phosphotransferase-like protein
crystal structure of atu3015, a putative cytidylate kinase from agrobacterium tumefaciens, northeast structural genomics target atr62
Identifiers
Symbol	CPT
Pfam	PF07931
Pfam clan	CL0023
InterPro	IPR012853
SCOP	1grq
Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure 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

1. ^ Izard T (August 2001). "Structural basis for chloramphenicol tolerance in Streptomyces venezuelae by chloramphenicol phosphotransferase activity". Protein Sci. 10 (8): 1508–13. doi:10.1002/pro.101508. PMC 2374082. PMID 11468347. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2374082. 
2. ^ Izard T, Ellis J (June 2000). "The crystal structures of chloramphenicol phosphotransferase reveal a novel inactivation mechanism". EMBO J. 19 (11): 2690–700. doi:10.1093/emboj/19.11.2690. PMC 212772. PMID 10835366. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=212772. 

This article includes text from the public domain Pfam and InterPro IPR012853