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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2009-5-18
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pubmed:databankReference |
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pubmed:abstractText |
The MogR transcriptional repressor of the intracellular pathogen Listeria monocytogenes recognizes AT-rich binding sites in promoters of flagellar genes to downregulate flagellar gene expression during infection. We describe here the 1.8 A resolution crystal structure of MogR bound to the recognition sequence 5' ATTTTTTAAAAAAAT 3' present within the flaA promoter region. Our structure shows that MogR binds as a dimer. Each half-site is recognized in the major groove by a helix-turn-helix motif and in the minor groove by a loop from the symmetry-related molecule, resulting in a "crossover" binding mode. This oversampling through minor groove interactions is important for specificity. The MogR binding site has structural features of A-tract DNA and is bent by approximately 52 degrees away from the dimer. The structure explains how MogR achieves binding specificity in the AT-rich genome of L. monocytogenes and explains the evolutionary conservation of A-tract sequence elements within promoter regions of MogR-regulated flagellar genes.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-10331874,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-10346815,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-10966775,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-11323673,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-11410653,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-11438706,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-12717729,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-12824317,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-12930962,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-14739342,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-15299374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-15302931,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-15488392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-15510218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-15546667,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-15572765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-15950122,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-15956202,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-16617375,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-1682054,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-16891416,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-17981120,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-18059448,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-18432246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-1977522,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-2025413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-3419502,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-3553959,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-7678431,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-7761829,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-7984417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-8662544,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19446532-9757107
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
769-77
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pubmed:dateRevised |
2010-9-27
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pubmed:meshHeading |
pubmed-meshheading:19446532-AT Rich Sequence,
pubmed-meshheading:19446532-Bacterial Proteins,
pubmed-meshheading:19446532-Base Sequence,
pubmed-meshheading:19446532-Binding Sites,
pubmed-meshheading:19446532-DNA,
pubmed-meshheading:19446532-DNA, Bacterial,
pubmed-meshheading:19446532-Flagellin,
pubmed-meshheading:19446532-Helix-Turn-Helix Motifs,
pubmed-meshheading:19446532-Listeria monocytogenes,
pubmed-meshheading:19446532-Models, Molecular,
pubmed-meshheading:19446532-Molecular Sequence Data,
pubmed-meshheading:19446532-Nucleic Acid Conformation,
pubmed-meshheading:19446532-Promoter Regions, Genetic,
pubmed-meshheading:19446532-Protein Conformation,
pubmed-meshheading:19446532-Repressor Proteins
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pubmed:year |
2009
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pubmed:articleTitle |
Recognition of AT-rich DNA binding sites by the MogR repressor.
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pubmed:affiliation |
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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