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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5434
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pubmed:dateCreated |
1999-10-8
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pubmed:abstractText |
To characterize the mechanism by which receptors propagate conformational changes across membranes, nitroxide spin labels were attached at strategic positions in the bacterial aspartate receptor. By collecting the electron paramagnetic resonance spectra of these labeled receptors in the presence and absence of the ligand aspartate, ligand binding was shown to generate an approximately 1 angstrom intrasubunit piston-type movement of one transmembrane helix downward relative to the other transmembrane helix. The receptor-associated phosphorylation cascade proteins CheA and CheW did not alter the ligand-induced movement. Because the piston movement is very small, the ability of receptors to produce large outcomes in response to stimuli is caused by the ability of the receptor-coupled enzymes to detect small changes in the conformation of the receptor.
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pubmed:grant |
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pubmed:commentsCorrections |
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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/Aspartic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/CheW protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/CheW protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Lipid Bilayers,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Amino Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Spin Labels,
http://linkedlifedata.com/resource/pubmed/chemical/aspartic acid receptor,
http://linkedlifedata.com/resource/pubmed/chemical/methyl-accepting chemotaxis proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
285
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1751-4
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10481014-Aspartic Acid,
pubmed-meshheading:10481014-Bacterial Proteins,
pubmed-meshheading:10481014-Cell Membrane,
pubmed-meshheading:10481014-Chemotaxis,
pubmed-meshheading:10481014-Dimerization,
pubmed-meshheading:10481014-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:10481014-Escherichia coli,
pubmed-meshheading:10481014-Escherichia coli Proteins,
pubmed-meshheading:10481014-Fourier Analysis,
pubmed-meshheading:10481014-Ligands,
pubmed-meshheading:10481014-Lipid Bilayers,
pubmed-meshheading:10481014-Membrane Proteins,
pubmed-meshheading:10481014-Methylation,
pubmed-meshheading:10481014-Models, Biological,
pubmed-meshheading:10481014-Mutagenesis,
pubmed-meshheading:10481014-Phosphorylation,
pubmed-meshheading:10481014-Protein Conformation,
pubmed-meshheading:10481014-Protein Kinases,
pubmed-meshheading:10481014-Protein Structure, Secondary,
pubmed-meshheading:10481014-Receptors, Amino Acid,
pubmed-meshheading:10481014-Signal Transduction,
pubmed-meshheading:10481014-Spin Labels
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pubmed:year |
1999
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pubmed:articleTitle |
A piston model for transmembrane signaling of the aspartate receptor.
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pubmed:affiliation |
Department of Molecular and Cell Biology and Department of Chemistry, University of California, Berkeley, CA 94720, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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