结核分枝杆菌鸟氨酸乙酰转移酶（Rv1653）的初步X射线晶体学分析。
Preliminary X-ray crystallographic analysis of ornithine acetyltransferase (Rv1653) from Mycobacterium tuberculosis.
作者信息
Sankaranarayanan R, Garen C R, Cherney M M, Yuan M, Lee C, James M N G
机构信息
Protein Structure and Function Group, Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Feb 1;65(Pt 2):173-6. doi: 10.1107/S1744309109000360. Epub 2009 Jan 31.
The gene product of open reading frame Rv1653 from Mycobacterium tuberculosis is annotated as encoding a probable ornithine acetyltransferase (OATase; EC 2.3.1.35), an enzyme that catalyzes two steps in the arginine-biosynthesis pathway. It transfers an acetyl group from N-acetylornithine to L-glutamate to produce N-acetylglutamate and L-ornithine. Rv1653 was crystallized using the sitting-drop vapour-diffusion method. The native crystals diffracted to a resolution of 1.7 A and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 60.1, b = 99.7, c = 155.3 A. The preliminary X-ray study showed the presence of a dimer in the asymmetric unit of the crystals, which had a Matthews coefficient V(M) of 2.8 A(3) Da(-1).
结核分枝杆菌开放阅读框Rv1653的基因产物被注释为可能编码鸟氨酸乙酰转移酶（OATase；EC 2.3.1.35），该酶在精氨酸生物合成途径中催化两个步骤。它将乙酰基从N - 乙酰鸟氨酸转移到L - 谷氨酸，生成N - 乙酰谷氨酸和L - 鸟氨酸。采用坐滴气相扩散法使Rv1653结晶。天然晶体的衍射分辨率为1.7 Å，属于空间群P2(1)2(1)2(1)，晶胞参数a = 60.1，b = 99.7，c = 155.3 Å。初步X射线研究表明，晶体的不对称单元中存在一个二聚体，其马修斯系数V(M)为2.8 ų Da⁻¹。
Zotero 插件