Linked Life Data

18725229

Source:http://linkedlifedata.com/resource/pubmed/id/18725229

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-9-22
pubmed:databankReference
pubmed:abstractText
C(4)-dicarboxylates are the major carbon and energy sources during the symbiotic growth of rhizobia. Responses to C(4)-dicarboxylates depend on typical two-component systems (TCS) consisting of a transmembrane sensor histidine kinase and a cytoplasmic response regulator. The DctB-DctD system is the first identified TCS for C(4)-dicarboxylates sensing. Direct ligand binding to the sensor domain of DctB is believed to be the first step of the sensing events. In this report, the water-soluble periplasmic sensor domain of Sinorhizobium meliloti DctB (DctBp) was studied, and three crystal structures were solved: the apo protein, a complex with C(4) succinate, and a complex with C(3) malonate. Different from the two structurally known CitA family of carboxylate sensor proteins CitA and DcuS, the structure of DctBp consists of two tandem Per-Arnt-Sim (PAS) domains and one N-terminal helical region. Only the membrane-distal PAS domain was found to bind the ligands, whereas the proximal PAS domain was empty. Comparison of DctB, CitA, and DcuS suggests a detailed stereochemistry of C(4)-dicarboxylates ligand perception. The structures of the different ligand binding states of DctBp also revealed a series of conformational changes initiated upon ligand binding and propagated to the N-terminal domain responsible for dimerization, providing insights into understanding the detailed mechanism of the signal transduction of TCS histidine kinases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1089-8638
pubmed:author
pubmed:issnType
Electronic
pubmed:day
31
pubmed:volume
383
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
49-61
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:18725229-Amino Acid Sequence, pubmed-meshheading:18725229-Bacterial Proteins, pubmed-meshheading:18725229-Crystallography, X-Ray, pubmed-meshheading:18725229-Dicarboxylic Acid Transporters, pubmed-meshheading:18725229-Dicarboxylic Acids, pubmed-meshheading:18725229-Dimerization, pubmed-meshheading:18725229-Escherichia coli Proteins, pubmed-meshheading:18725229-Ligands, pubmed-meshheading:18725229-Models, Molecular, pubmed-meshheading:18725229-Molecular Sequence Data, pubmed-meshheading:18725229-Protein Conformation, pubmed-meshheading:18725229-Protein Kinases, pubmed-meshheading:18725229-Protein Structure, Quaternary, pubmed-meshheading:18725229-Protein Structure, Tertiary, pubmed-meshheading:18725229-Sequence Homology, Amino Acid, pubmed-meshheading:18725229-Signal Transduction, pubmed-meshheading:18725229-Sinorhizobium meliloti
pubmed:year
2008
pubmed:articleTitle
C4-dicarboxylates sensing mechanism revealed by the crystal structures of DctB sensor domain.
pubmed:affiliation
National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing 100871, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't