Cloning, purification, crystallization and preliminary crystallographic analysis of LsrR from Escherichia coli.
In Escherichia coli, the lsr operon is composed of six genes lsrACDBFG which regulate uptake and modification of the signalling molecule AI-2. LsrR is a repressor of the lsr operon and itself, which can bind phospho-AI-2 and be released from the promoter region of the operon and thus activate gene expression. LsrR fused with an HHHHHH sequence at the C-terminus was expressed, purified and crystallized in order to determine its structure and elucidate the molecular mechanism of repression. The crystal belonged to space group I222, with unit-cell parameters a=79.84, b=116.65, c=186.04 A, and was estimated to contain two protein molecules per asymmetric unit.
Liu
Xiaotian
X
School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230027, People's Republic of China.
Wu
Minhao
M
Sun
Demeng
D
Zang
Jianye
J
D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D012097:Repressor Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
D029968:Escherichia coli Proteins; C504601:LsrR protein, E coli; D012097:Repressor Proteins