Publication Abstract from PubMed
Peptide deformylase (PDF) is a metalloenzyme that removes the N-terminal formyl groups from newly synthesized proteins. It is essential for bacterial survival, and is therefore-considered as a potential target for antimicrobial chemotherapy. However, some bacteria including medically relevant pathogens possess two or more def-like genes. Here we have examined two PDFs from Bacillus cereus. The two share only 32% sequence identity and the crystal structures show overall similarity with PDF2 having a longer C-terminus. However, there are differences at the two active sites, and these differences appear to contribute to the activity difference seen between the two. BcPDF2 is found as a dimer in the crystal form with two additional actinonin bound at that interface.
Characterization of peptide deformylase2 from B. cereus.,Park JK, Kim KH, Moon JH, Kim EE J Biochem Mol Biol. 2007 Nov 30;40(6):1050-7. PMID:18047803[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
