嗜热栖热菌天冬氨酸激酶调节亚基的纯化、结晶及初步X射线分析
Purification, crystallization and preliminary X-ray analysis of the regulatory subunit of aspartate kinase from Thermus thermophilus.
作者信息
Yoshida Ayako, Tomita Takeo, Kuzuyama Tomohisa, Nishiyama Makoto
机构信息
Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Feb 1;63(Pt 2):96-8. doi: 10.1107/S1744309106055837. Epub 2007 Jan 17.
Abstract
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 beta subunit of T. thermophilus AK) was crystallized in the presence of the inhibitor threonine. Diffraction data were collected to 2.15 A at a synchrotron source. The crystal belongs to the cubic space group P4(3)32 or P4(1)32, with unit-cell parameters a = b = c = 141.8 A.
摘要
嗜热栖热菌的天冬氨酸激酶（AK）催化苏氨酸和蛋氨酸生物合成的第一步，它受终产物苏氨酸的反馈抑制调节。为阐明AK的调节机制，在抑制剂苏氨酸存在的情况下，对调节亚基（嗜热栖热菌AK的β亚基）进行了结晶。在同步加速器光源处收集到了分辨率为2.15 Å的衍射数据。晶体属于立方晶系空间群P4(3)32或P4(1)32，晶胞参数a = b = c = 141.8 Å。
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