Crystallization and Preliminary X-ray Diffraction Study of Phosphoribosyl Pyrophosphate Synthetase from E-Coli

被引：1
|
作者：
Timofeev, V. I. [1 ,2 ]
Abramchik, Yu. A. [1 ,3 ]
Zhukhlistova, N. E. [1 ]
Kuranova, I. P. [1 ,2 ]
机构：
[1] Russian Acad Sci, Shubnikov Inst Crystallog, Moscow 119333, Russia
[2] Kurchatov Inst, Natl Res Ctr, Moscow 123098, Russia
[3] Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia
来源：
CRYSTALLOGRAPHY REPORTS | 2015年 / 60卷 / 05期
基金：
俄罗斯基础研究基金会;
关键词：
COUNTER-DIFFUSION METHOD; DIPHOSPHATE SYNTHETASE; SALMONELLA-TYPHIMURIUM; RIBOSE; 5-PHOSPHATE; BACILLUS-SUBTILIS; CRYSTAL-GROWTH; ENZYME; PURIFICATION; GENE; MECHANISM;
D O I：
10.1134/S1063774515050181
中图分类号：
O7 [晶体学];
学科分类号：
0702 ; 070205 ; 0703 ; 080501 ;
摘要：
Enzymes of the phosphoribosyl pyrophosphate synthetase family (PRPPS, EC 2.7.6.1) catalyze the formation of 5-phosphoribosyl pyrophosphate (5-PRPP) from adenosine triphosphate and ribose 5-phosphate. 5-Phosphoribosyl pyrophosphate is an important intermediate in the synthesis of purine, pyrimidine, and pyridine nucleotides, as well as of the amino acids histidine and tryptophan. The crystallization conditions for E. coli PRPPS were found by the vapor-diffusion technique and were optimized to apply the capillary counter-diffusion technique. The X-ray diffraction data set was collected from the crystals grown by the counter-diffusion technique using a synchrotron radiation source to 3.1-angstrom resolution. The crystals of PRPPS belong to sp. gr. P6(3)22 and have the following unit-cell parameters: a = b = 104.44 angstrom, c = 124.98 angstrom , alpha = beta = 90 degrees, gamma = 120 degrees. The collected X-ray diffraction data set is suitable for the solution of the three-dimensional structure of PRPPS at 3.1-angstrom resolution.
引用
收藏
页码：685 / 688
页数：4
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