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Crystal structure of the transcriptional regulator CmeR from Campylobacter jejuni.

Crystal structure of the transcriptional regulator CmeR from Campylobacter jejuni. Research Abstract Details 

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  • Crystal structure of the transcriptional regulator CmeR from Campylobacter jejuni. Abstract Text:

    ruoyu guRuoyu Gu,chih-chia suChih-Chia Su,feng shiFeng Shi,ming liMing Li,gerry mcdermottGerry McDermott,qijing zhangQijing Zhang,edward w yuEdward W Yu,ruoyu guRuoyu Gu,chih-chia suChih-Chia Su,feng shiFeng Shi,ming liMing Li,gerry mcdermottGerry McDermott,qijing zhangQijing Zhang,edward w yuEdward W Yu,

    The CmeABC multidrug efflux pump, which belongs to the resistance-nodulation-division (RND) family, recognizes and extrudes a broad range of antimicrobial agents and is essential for Campylobacter jejuni colonization of the animal intestinal tract by mediating the efflux of bile acids. The expression of CmeABC is controlled by the transcriptional regulator CmeR, whose open reading frame is located immediately upstream of the cmeABC operon. To understand the structural basis of CmeR regulation, we have determined the crystal structure of CmeR to 2.2 A resolution, revealing a dimeric two-domain molecule with an entirely helical architecture similar to members of the TetR family of transcriptional regulators. Unlike the rest of the TetR regulators, CmeR has a large center-to-center distance (54 A) between two N termini of the dimer, and a large flexible ligand-binding pocket in the C-terminal domain. Each monomer forms a 20 A long tunnel-like cavity in the ligand-binding domain of CmeR and is occupied by a fortuitous ligand that is identified as glycerol. The binding of glycerol to CmeR induces a conformational state that is incompatible with target DNA. As glycerol has a chemical structure similar to that of potential ligands of CmeR, the structure obtained mimics the induced form of CmeR. These findings reveal novel structural features of a TetR family regulator, and provide new insight into the mechanisms of ligand binding and CmeR regulation.

    Crystal structure of the transcriptional regulator CmeR from Campylobacter jejuni. Publishing Authors By Initials

    r guR Gu,cc suCC Su,f shiF Shi,m liM Li,g mcdermottG McDermott,q zhangQ Zhang,ew yuEW Yu,r guR Gu,cc suCC Su,f shiF Shi,m liM Li,g mcdermottG McDermott,q zhangQ Zhang,ew yuEW Yu,

    For similar proteins: transcription factors research abstracts see: proteins: transcription factors research

    PUBMED ID PMID:

    MEDLINE DATE:

    Crystal structure of the transcriptional regulator CmeR from Campylobacter jejuni. Journal Published:

    PUBLICATION TYPE: Research Support, N.I.H., Extr

    Journal: Journal of molecular biology

    VOLUME: 372

    Page Numbers: 583-93

    Journal Abbreviation: J. Mol. Biol.

    ISSN: 0022-2836

    DAY: 3

    MONTH: 07

    YEAR: 2007

    Crystal structure of the transcriptional regulator CmeR from Campylobacter jejuni. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 2985088

    Crystal structure of the transcriptional regulator CmeR from Campylobacter jejuni. Keywords Mesh Terms:

    KEYWORDS: Transcription Factors

    MESH TERMS: chemistry

    Chemical & Substance for Abstract: Crystal structure of the transcriptional regulator CmeR from Campylobacter jejuni. Information

    Substance Name: Glycerol

    Registry Number: 56-81-5

    Grant and Affiliation Information for Crystal structure of the transcriptional regulator CmeR from Campylobacter jejuni.

    AFFILIATION: Department of Physics and Astronomy, Iowa State University, Ames, IA 50011, USA.

    Country: England

    England Research PublicationEngland Research Publication

    AGENCY: United States NIGMS

    GRANT: GM074027

    ACRONYM: GM

    MEDLINETA: J Mol Biol

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

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