Purification, crystallization and preliminary X-ray crystallographic analysis of the C-terminal cytoplasmic domain of FlhB from Salmonella typhimurium

被引:2
|
作者
Meshcheryakov, Vladimir A. [1 ]
Samatey, Fadel A. [1 ]
机构
[1] Okinawa Inst Sci & Technol, Transmembrane Trafficking Unit, Onna Son, Okinawa 9040412, Japan
关键词
FLAGELLAR EXPORT APPARATUS; HOOK-LENGTH CONTROL; III SECRETION SYSTEMS; SUBSTRATE-SPECIFICITY; BACTERIAL FLAGELLA; AQUIFEX-AEOLICUS; FLIK; COMPONENTS; SWITCH; YSCU;
D O I
10.1107/S1744309111018938
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
FlhB is a key protein in the regulation of protein export by the bacterial flagellar secretion system. It is composed of two domains: an N-terminal transmembrane domain and a C-terminal cytoplasmic domain (FlhBc). FlhBc from Salmonella typhimurium has been successfully crystallized using the vapour-diffusion method. The crystals diffracted to 2.45 angstrom resolution and belonged to space group P4(2)2(1)2, with unit-cell parameters a = b = 49.06, c = 142.94 angstrom. A selenomethionine-containing variant of FlhBc has also been crystallized in the same space group and was used for initial phase calculation by the multiwavelength anomalous dispersion (MAD) method.
引用
收藏
页码:808 / 811
页数:4
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