Open AccessExpression, crystallization and preliminary crystallographic studies of a novel bifunctional N ‐acetylglutamate synthase/kinase from Xanthomonas campestris homologous to vertebrate N ‐acetylglutamate synthase
Author(s) -
Shi Dashuang,
Caldovic Ljubica,
Jin Zhongmin,
Yu Xiaolin,
Qu Qiuhao,
Roth Lauren,
Morizono Hiroki,
Hathout Yetrib,
Allewell Norma M.,
Tuchman Mendel
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106044101
Subject(s) - atp synthase , xanthomonas campestris , biology , biosynthesis , biochemistry , phosphofructokinase 2 , microbiology and biotechnology , enzyme , gene
A novel N ‐acetylglutamate synthase/kinase bifunctional enzyme of arginine biosynthesis that was homologous to vertebrate N ‐acetylglutamate synthases was identified in Xanthomonas campestris . The protein was overexpressed, purified and crystallized. The crystals belong to the hexagonal space group P 6 2 22, with unit‐cell parameters a = b = 134.60, c = 192.11 Å, and diffract to about 3.0 Å resolution. Selenomethionine‐substituted recombinant protein was produced and selenomethionine substitution was verified by mass spectroscopy. Multiple anomalous dispersion (MAD) data were collected at three wavelengths at SER‐CAT, Advanced Photon Source, Argonne National Laboratory. Structure determination is under way using the MAD phasing method.