Open AccessCloning, expression, crystallization and preliminary X‐ray crystallographic analysis of 3‐dehydroquinate synthase, Xoo1243, from Xanthomonas oryzae pv. oryzae
Author(s) -
Ngo PhuongThuy Ho,
Natarajan Sampath,
Kim Hyesoon,
Hung Huynh Kim,
Kim JeongGu,
Lee ByoungMoo,
Ahn YehJin,
Kang LinWoo
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108033575
Subject(s) - xanthomonas oryzae pv. oryzae , xanthomonas oryzae , crystallization , atp synthase , cloning (programming) , xanthomonas , biology , crystallography , microbiology and biotechnology , chemistry , enzyme , genetics , biochemistry , gene , computer science , organic chemistry , programming language , pathogen
The disease bacterial blight results in serious production losses of rice in Asian countries. The aroB gene encoding dehydroquinate synthase (DHQS), which is a potential antibiotic target, was identified from the plant‐pathogenic bacterium Xanthomonas oryzae pv. oryzae (Xoo). DHQS plays an essential role in the synthesis of aromatic compounds in the shikimate pathway. The aroB gene (Xoo1243) was cloned from Xoo and the corresponding DHQS protein was subsequently overexpressed in Escherichia coli . The purified protein was crystallized using the hanging‐drop vapour‐diffusion method and yielded crystals that diffracted to 2.5 Å resolution. The crystals belonged to the tetragonal space group P 4 3 2 1 2, with unit‐cell parameters a = b = 118.2, c = 98.2 Å. According to a Matthews coefficient calculation, the crystal contained two molecules in the asymmetric unit, with a corresponding V M of 2.06 Å 3 Da −1 and a solvent content of 40.4%.