Buss K A, Ingram-Smith C, Ferry J G, Sanders D A, Hasson M S
Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907-1392, USA.
Protein Sci. 1997 Dec;6(12):2659-62. doi: 10.1002/pro.5560061222.
The unique biochemical properties of acetate kinase present a classic conundrum in the study of the mechanism of enzyme-catalyzed phosphoryl transfer. Large, single crystals of acetate kinase from Methanosarcina thermophila were grown from a solution of ammonium sulfate in the presence of ATP. The crystals diffract to beyond 1.7 A resolution. Analysis of X-ray data from the crystals is consistent with a space group of C2 and unit cell dimensions a = 181 A, b = 67 A, c = 83 A, beta = 103 degrees. Diffraction data have been collected from the crystals at 110 and 277 K. Data collected at 277 K extend to lower resolution, but are more reproducible. The orientation of a noncrystallographic two-fold axis of symmetry has been determined. Based on an analysis of the predicted amino acid sequences of acetate kinase from several organisms, we hypothesize that acetate kinase is a member of the sugar kinase/actin/hsp70 structural family.
嗜热甲烷八叠球菌乙酸激酶独特的生化特性在酶催化磷酸基转移机制的研究中呈现出一个经典难题。嗜热甲烷八叠球菌乙酸激酶的大单晶是在ATP存在的情况下从硫酸铵溶液中生长出来的。这些晶体的衍射分辨率超过1.7埃。对晶体X射线数据的分析与空间群C2以及晶胞尺寸a = 181埃、b = 67埃、c = 83埃、β = 103°一致。已在110K和277K下从晶体收集衍射数据。在277K收集的数据分辨率较低，但重复性更好。已确定了一个非晶体学二重对称轴的取向。基于对几种生物体中乙酸激酶预测氨基酸序列的分析，我们推测乙酸激酶是糖激酶/肌动蛋白/hsp70结构家族的成员。
