Article info Vol. 5  No. 1   pp.  49 ~ 52
Title Expression, crystallization, and preliminary X-ray crystallographic analysis of peptide deformylase from Acinetobacter baumanii
Authors Thien-Hoang Ho 1,+ , Kyoungho Jung 1,+ , Inho Lee 1 , Kim-Hung Huynh 1 , Diem-Quynh Nguyen 1 , Hyunjae Park 1 , Sang Hee Lee 2 and Lin-Woo Kang 1, *
Institutions 1 Department of Biological Sciences, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul 05029, Korea, 2 National Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, 116 Myongjiro, Yongin, Gyeonggido 17058, Korea. *Correspondence: lkang@konkuk.ac.kr + These authors contribute equally for this paper.
Abstract The emergences of multi-drug resistant bacteria such as Acinetobacter baumanni have emphasized the necessity of new antibiotics. Peptidyl deformylase (PDF) catalyzes the removal of the formyl group from the N-terminal formylated methionine residue present in all nascent polypeptides in bacteria. In this study, the PDF gene from Acinetobacter baumannii K0420859 was cloned and its protein was overexpressed in E. coli, purified, and crystallized. The purified protein was crystallized using the hanging-drop vapour-diffusion method and the crystal diffracted to 2.4 Å resolution. The crystal belonged to the trigonal space group P3 2 with unit cell parameters of a = b= 39.4 Å and c = 187.9 Å. Two protomers were presented in the asymmetric unit with a corresponding V M of 2.10 Å 3 Da -1 and a solvent content of 41.5%.