Purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal fragment of the MvfR protein from Pseudomonas aeruginosa

被引：9

作者：

Kefala, Katerina ^{[1
]}

Kotsifaki, Dina ^{[2
]}

Providaki, Mary ^{[2
]}

Kapetaniou, Evangelia G. ^{[2
]}

Rahme, Lawrence ^{[3
,4
]}

Kokkinidis, Michael ^{[1
,2
]}

机构：

[1] Univ Crete, Dept Biol, GR-71003 Iraklion, Crete, Greece

[2] Inst Mol Biol & Biotechnol, GR-71110 Iraklion, Crete, Greece

[3] Harvard Univ, Massachusetts Gen Hosp, Sch Med, Dept Surg, Boston, MA USA

[4] Massachusetts Gen Hosp, Shriners Burns Inst, Boston, MA 02114 USA

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2012年 / 68卷

关键词：

MvfR; LysR-type transcriptional regulators; Pseudomonas aeruginosa; TO-CELL COMMUNICATION; GENE; REGULATOR;

D O I：

10.1107/S1744309112016661

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：695 / 697

页数：3

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