Crystallization and preliminary X-ray analysis of pyruvate kinase from Bacillus stearothermophilus

被引：1
|
作者：
Suzuki, K [1 ]
Ito, S [1 ]
ShIbuka, AS [1 ]
Shimizu-Ibuka, A [1 ]
Sakai, H [1 ]
机构：
[1] Univ Shizuoka, Dept Food & Nutr Sci, Shizuoka 4228526, Japan
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2005年 / 61卷
关键词：
D O I：
10.1107/S1744309105021093
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
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 angstrom.
引用
收藏
页码：759 / 761
页数：3
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