Source:http://linkedlifedata.com/resource/pubmed/id/20149110
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2010-5-21
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pubmed:abstractText |
Sinorhizobium meliloti DctB is a typical transmembrane sensory histidine kinase, which senses C(4)-dicarboxylic acids (DCA) and regulates the expression of DctA, the DCA transporter. We previously reported the crystal structures of its periplasmic sensory domain (DctBp) in apo and succinate-bound states, and these structures showed dramatic conformational changes at dimeric level. Here we show a ligand-induced dimeric switch in solution and a strong correlation between DctBp's dimerization states and the in vivo activities of DctB. Using site-directed mutagenesis, we identify important determinants for signal perception and transduction. Specifically, we show that the ligand-binding pocket is essential for DCA-induced 'on' activity of DctB. Mutations at different sections of DctBp's dimerization interface can lock full-length DctB at either 'on' or 'off' state, independent of ligand binding. Taken together, these results suggest that DctBp's signal perception and transduction occur through a 'ligand-induced dimeric switch', in which the changes in the dimeric conformations upon ligand binding are responsible for the signal transduction in DctB.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DCTB protein, Sinorhizobium,
http://linkedlifedata.com/resource/pubmed/chemical/Dicarboxylic Acid Transporters,
http://linkedlifedata.com/resource/pubmed/chemical/Dicarboxylic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Mutant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1365-2958
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
75
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1484-94
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pubmed:meshHeading |
pubmed-meshheading:20149110-Amino Acid Substitution,
pubmed-meshheading:20149110-Bacterial Proteins,
pubmed-meshheading:20149110-Dicarboxylic Acid Transporters,
pubmed-meshheading:20149110-Dicarboxylic Acids,
pubmed-meshheading:20149110-Dimerization,
pubmed-meshheading:20149110-Models, Molecular,
pubmed-meshheading:20149110-Mutagenesis, Site-Directed,
pubmed-meshheading:20149110-Mutant Proteins,
pubmed-meshheading:20149110-Protein Conformation,
pubmed-meshheading:20149110-Protein Structure, Quaternary,
pubmed-meshheading:20149110-Protein Structure, Tertiary,
pubmed-meshheading:20149110-Signal Transduction,
pubmed-meshheading:20149110-Sinorhizobium meliloti
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pubmed:year |
2010
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pubmed:articleTitle |
From signal perception to signal transduction: ligand-induced dimeric switch of DctB sensory domain in solution.
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pubmed:affiliation |
National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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