嗜热脂肪芽孢杆菌丙酮酸激酶的结晶及初步X射线分析
Crystallization and preliminary X-ray analysis of pyruvate kinase from Bacillus stearothermophilus.
作者信息
Suzuki Kenichiro, Ito Sohei, Shimizu-Ibuka Akiko, Sakai Hiroshi
机构信息
Department of Food and Nutritional Sciences, University of Shizuoka, Yada 52-1, Shizuoka 422-8526, Japan.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Aug 1;61(Pt 8):759-61. doi: 10.1107/S1744309105021093. Epub 2005 Jul 30.
Pyruvate kinase (PK) from a moderate thermophile, Bacillus stearothermophilus (BstPK), is an allosteric enzyme activated by AMP and ribose 5-phosphate but not by fructose 1,6-bisphosphate (FBP). However, almost all other PKs are activated by FBP. The wild-type and W416F/V435W mutant BstPKs were crystallized by the hanging-drop vapour-diffusion method. However, they were unsuitable for structural analysis because their data sets exhibited low completeness. A crystal suitable for structural analysis was obtained using C9S/C268S enzyme. The crystal belonged to space group P6(2)22, with unit-cell parameters a = b = 145.97, c = 118.03 A.
来自嗜热栖热芽孢杆菌（BstPK）的丙酮酸激酶（PK）是一种别构酶，可被AMP和5-磷酸核糖激活，但不能被1,6-二磷酸果糖（FBP）激活。然而，几乎所有其他PK都被FBP激活。野生型和W416F/V435W突变型BstPK通过悬滴气相扩散法结晶。然而，它们不适合进行结构分析，因为其数据集的完整性较低。使用C9S/C268S酶获得了适合结构分析的晶体。该晶体属于空间群P6(2)22，晶胞参数a = b = 145.97，c = 118.03 Å。
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