猪心脏柠檬酸合酶在1.78埃分辨率下的结构。
Structure of pig heart citrate synthase at 1.78 A resolution.
作者信息
Larson Steven B, Day John S, Nguyen Chieugiang, Cudney Robert, McPherson Alexander
机构信息
Department of Molecular Biology and Biochemistry, The University of California, Irvine, 92697-3900, USA.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 May 1;65(Pt 5):430-4. doi: 10.1107/S1744309109008343. Epub 2009 Apr 24.
Abstract
Pig heart citrate synthase was crystallized from a small-molecule cocktail containing cystamine dihydrochloride, aspartame and benzamidine hydrochloride. The structure was refined to an R factor of 0.179 (R(free) = 0.222) using synchrotron data to a resolution of 1.78 A. The model includes the full-length protein, a chloride ion, a sulfate ion, 305 water molecules and an unexpected moiety attached through a disulfide linkage to Cys184, which was modeled as a half-cystamine molecule generated by disulfide exchange with the cystamine in the small-molecule cocktail.
摘要
猪心脏柠檬酸合酶是从含有二盐酸半胱胺、阿斯巴甜和盐酸苯甲脒的小分子混合液中结晶出来的。利用同步加速器数据将结构精修至分辨率为1.78 Å，R因子为0.179（R（自由）= 0.222）。该模型包括全长蛋白质、一个氯离子、一个硫酸根离子、305个水分子以及通过二硫键连接到Cys184的一个意外部分，该部分被模拟为通过与小分子混合液中的半胱胺进行二硫键交换生成的半胱胺分子。
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