Expression, crystallization and preliminary X-ray crystallographic analysis of peptide deformylase from Xanthomonas oryzae pv. oryzae.
Peptide deformylase (PDF) catalyzes the removal of the N-formyl group from the N-terminus of newly synthesized polypeptides; this process is crucial for cell survival. As it is an antibacterial drug target against Xanthomonas oryzae pv. oryzae (Xoo), PDF from Xoo was cloned, expressed, purified and crystallized. Native PDF crystals diffracted to 2.7 A resolution and belonged to the hexagonal space group P6(1)22, with unit-cell parameters a = b = 59.0, c = 266.3 A. One monomer is present in the asymmetric unit, with a corresponding crystal volume per protein weight of 3.50 A(3) Da(-1) and a solvent content of 64.9%.
Ngo
Phuong-Thuy Ho
PT
Department of Advanced Technology Fusion, Konkuk University, Hwayang-dong, Gwangjin-gu, Seoul 143-701, Republic of Korea.
Kim
Jin-Kwang
JK
Kim
Hyesoon
H
Jung
Junho
J
Ahn
Yeh-Jin
YJ
Kim
Jeong-Gu
JG
Lee
Byoung-Moo
BM
Kang
Lin-Woo
LW
D000581:Amidohydrolases / Q000737:chemistry* / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D012275:Oryza / Q000382:microbiology; D014974:Xanthomonas / Q000201:enzymology*
D001426:Bacterial Proteins; D000581:Amidohydrolases; C084507:peptide deformylase