Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2010-5-21
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1365-2958
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
75
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1484-94
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
From signal perception to signal transduction: ligand-induced dimeric switch of DctB sensory domain in solution.
pubmed:affiliation
National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't