2okl | pdb_00002okl
|
Crystal structure of Peptide Deformylase 2 with actinonin from Bacillus cereus
Overview
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.
About this Structure
2OKL is a Single protein structure of sequence from Bacillus cereus with ZN, BB2 and CIT as ligands. Active as Peptide deformylase, with EC number 3.5.1.88 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Jan 23 11:05:57 2008
