铜绿假单胞菌MvfR蛋白C端片段的纯化、结晶及初步X射线衍射分析
Purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal fragment of the MvfR protein from Pseudomonas aeruginosa.
作者信息
Kefala Katerina, Kotsifaki Dina, Providaki Mary, Kapetaniou Evangelia G, Rahme Lawrence, Kokkinidis Michael
机构信息
Department of Biology, University of Crete, PO Box 2208, GR-71003 Heraklion, Crete, Greece.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jun 1;68(Pt 6):695-7. doi: 10.1107/S1744309112016661. Epub 2012 May 23.
Abstract
The LysR-type transcriptional regulator MvfR plays a critical role in Pseudomonas aeruginosa pathogenicity via the transcriptional regulation of multiple quorum-sensing-regulated virulence factors. The protein also controls pathogenic type VI secretion loci. MvfRC87, a 242-residue C-terminal segment of MvfR, was produced in Escherichia coli, purified and crystallized. X-ray diffraction data were collected using synchrotron radiation and crystallographic parameters were determined.
摘要
LysR 型转录调节因子 MvfR 通过对多种群体感应调节的毒力因子进行转录调控，在铜绿假单胞菌致病性中发挥关键作用。该蛋白还控制致病性 VI 型分泌位点。MvfRC87 是 MvfR 的一个由 242 个残基组成的 C 末端片段，在大肠杆菌中产生、纯化并结晶。使用同步辐射收集 X 射线衍射数据并确定晶体学参数。
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