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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2008-11-5
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pubmed:databankReference |
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pubmed:abstractText |
The sensor histidine kinase A (KinA) from Bacillus subtilis triggers a phosphorelay that activates sporulation. The antikinase KipI prevents sporulation by binding KinA and inhibiting the autophosphorylation reaction. Using neutron contrast variation, mutagenesis, and fluorescence data, we show that two KipI monomers bind via their C-domains at a conserved proline in the KinA dimerization and histidine-phosphotransfer (DHp) domain. Our crystal structure of the KipI C-domain reveals the binding motif has a distinctive hydrophobic groove formed by a five-stranded antiparallel beta-sheet; a characteristic of the cyclophilin family of proteins that bind prolines and often act as cis-trans peptidyl-prolyl isomerases. We propose that the DHp domain of KinA transmits conformational signals to regulate kinase activity via this proline-mediated interaction. Given that both KinA and KipI homologues are widespread in the bacterial kingdom, this mechanism has broad significance in bacterial signal transduction.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon-Sulfur Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclophilins,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/LuxS protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Peptidylprolyl Isomerase,
http://linkedlifedata.com/resource/pubmed/chemical/Proline,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Tryptophan,
http://linkedlifedata.com/resource/pubmed/chemical/protein-histidine kinase
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1089-8638
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
12
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pubmed:volume |
384
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
422-35
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:18823995-Amino Acid Sequence,
pubmed-meshheading:18823995-Bacillus subtilis,
pubmed-meshheading:18823995-Bacterial Proteins,
pubmed-meshheading:18823995-Carbon-Sulfur Lyases,
pubmed-meshheading:18823995-Crystallography, X-Ray,
pubmed-meshheading:18823995-Cyclophilins,
pubmed-meshheading:18823995-Dimerization,
pubmed-meshheading:18823995-Enzyme Inhibitors,
pubmed-meshheading:18823995-Models, Molecular,
pubmed-meshheading:18823995-Molecular Sequence Data,
pubmed-meshheading:18823995-Neutrons,
pubmed-meshheading:18823995-Peptidylprolyl Isomerase,
pubmed-meshheading:18823995-Proline,
pubmed-meshheading:18823995-Protein Kinases,
pubmed-meshheading:18823995-Protein Structure, Tertiary,
pubmed-meshheading:18823995-Quorum Sensing,
pubmed-meshheading:18823995-Scattering, Radiation,
pubmed-meshheading:18823995-Structural Homology, Protein,
pubmed-meshheading:18823995-Tryptophan,
pubmed-meshheading:18823995-X-Rays
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pubmed:year |
2008
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pubmed:articleTitle |
Histidine kinase regulation by a cyclophilin-like inhibitor.
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pubmed:affiliation |
School of Molecular and Microbial Biosciences, University of Sydney, Sydney, New South Wales 2006, Australia.
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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
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