PMID:20693666
| Citation |
Liu, X, Wu, M, Sun, D and Zang, J (2010) Cloning, purification, crystallization and preliminary crystallographic analysis of LsrR from Escherichia coli. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66:913-5 |
|---|---|
| Abstract |
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. |
| Links |
PubMed PMC2917289 Online version:10.1107/S1744309110020695 |
| Keywords |
Cloning, Molecular; Crystallization; Crystallography, X-Ray; Escherichia coli/chemistry; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/isolation & purification; Repressor Proteins/chemistry; Repressor Proteins/genetics; Repressor Proteins/isolation & purification |
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