Open AccessExpression, crystallization and preliminary X‐ray crystallographic analysis of peptide deformylase from Campylobacter jejuni
Author(s) -
Tran Huyen Thi,
Pham TanViet,
Ngo HoPhuongThuy,
Hong Myoungki,
Ahn YehJin,
Kang LinWoo
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113023506
Subject(s) - campylobacter jejuni , crystallization , methionine , peptide , monomer , gene , escherichia coli , biology , biochemistry , chemistry , bacteria , microbiology and biotechnology , stereochemistry , amino acid , organic chemistry , genetics , polymer
Campylobacter jejuni is one of the major foodborne pathogens causing human infection. Peptide deformylase, a metallohydrolase, catalyzes the deformylation of N ‐formylated methionine in newly synthesized polypeptides in prokaryotes and some eukaryotic organelles. The deformylation process is an essential step in protein synthesis and has attracted much attention as a potential target for the development of novel antibacterial agents. Here, the cloned codon‐optimized def gene from C. jejuni was synthesized and the protein was expressed, purified and crystallized. C. jejuni peptide deformylase crystals obtained at pH 7.0 and pH 6.5 diffracted to 2.9 Å resolution and belonged to the trigonal space group R 3, with unit‐cell parameters a = b = 105.7, c = 58.0 Å. One monomer existed in the asymmetric unit, with a corresponding V M of 3.1 Å 3 Da −1 and a solvent content of 60.4%.