Literature DB >> 20693666

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

Xiaotian Liu1, Minhao Wu, Demeng Sun, Jianye Zang.   

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.

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Year:  2010        PMID: 20693666      PMCID: PMC2917289          DOI: 10.1107/S1744309110020695

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  10 in total

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Authors:  Karina B Xavier; Bonnie L Bassler
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  10 in total
  1 in total

1.  Structural basis for phosphorylated autoinducer-2 modulation of the oligomerization state of the global transcription regulator LsrR from Escherichia coli.

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  1 in total

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