Open AccessPurification, crystallization and preliminary X‐ray analysis of the regulatory subunit of aspartate kinase from Thermus thermophilus
Author(s) -
Yoshida Ayako,
Tomita Takeo,
Kuzuyama Tomohisa,
Nishiyama Makoto
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106055837
Subject(s) - thermus thermophilus , protein subunit , threonine , biochemistry , crystallization , methionine , biology , crystallography , chemistry , enzyme , amino acid , serine , escherichia coli , gene , organic chemistry
Aspartate kinase (AK) from Thermus thermophilus , which catalyzes the first step of threonine and methionine biosynthesis, is regulated via feedback inhibition by the end product threonine. To elucidate the mechanism of regulation of AK, the regulatory subunit (the β subunit of T. thermophilus AK) was crystallized in the presence of the inhibitor threonine. Diffraction data were collected to 2.15 Å at a synchrotron source. The crystal belongs to the cubic space group P 4 3 32 or P 4 1 32, with unit‐cell parameters a = b = c = 141.8 Å.