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Cloning, purification, crystallization and preliminary crystallographic analysis of LsrR from Escherichia coli.

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.

SUBMITTER: Liu X

PROVIDER: S-EPMC2917289 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature

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Cloning, purification, crystallization and preliminary crystallographic analysis of LsrR from Escherichia coli.

Liu Xiaotian X Wu Minhao M Sun Demeng D Zang Jianye J

Acta crystallographica. Section F, Structural biology and crystallization communications 20100727 Pt 8

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 cr ...[more]

PMID: 20693666

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