Expression, purification, crystallization and preliminary diffraction analysis of CapF, a capsular polysaccharide-synthesis enzyme from Staphylococcus aureus

被引：5
|
作者：
Miyafusa, Takamitsu [1 ]
Tanaka, Yoshikazu [1 ,2 ]
Kuroda, Makoto [3 ]
Ohta, Toshiko [3 ]
Tsumoto, Kouhei [1 ]
机构：
[1] Univ Tokyo, Grad Sch Frontier Sci, Dept Med Genome Sci, Tokyo 2778562, Japan
[2] Hokkaido Univ, Sapporo, Hokkaido 0010021, Japan
[3] Univ Tsukuba, Grad Sch Comprehens Human Sci, Inst Basic Med Sci, Dept Microbiol, Tsukuba, Ibaraki 3058575, Japan
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2008年 / 64卷
关键词：
Capsular polysaccharide-synthesis enzymes; Differential scanning calorimetry; Staphylococcus aureus;
D O I：
10.1107/S174430910801213X
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Capsular polysaccharides (CPs) are important virulence factors of Staphylococcus aureus. The biosynthesis of type 5 and type 8 CPs (CP5 and CP8), which are produced by most clinical isolates of S. aureus, is catalyzed by 16 CP-assembling proteins. One of these proteins is the enzyme CapF, which catalyzes the synthesis of UDP-N-acetyl-L-fucosamine, a component of both CP5 and CP8. Here, the cloning, expression, purification, crystallization and diffraction analysis of CapF are reported. Optimization of the crystallization conditions by differential scanning calorimetry afforded a crystal of selenomethionine-substituted CapF that diffracted to a resolution of 2.80 angstrom. The crystal belongs to space group P3(2)21, with unit-cell parameters a = b = 119.6, c = 129.5 angstrom.
引用
收藏
页码：512 / 515
页数：4
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