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rdf:type |
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lifeskim:mentions |
umls-concept:C0014834,
umls-concept:C0024485,
umls-concept:C0072399,
umls-concept:C0183210,
umls-concept:C0205287,
umls-concept:C0220833,
umls-concept:C0445254,
umls-concept:C0678594,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2348081
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pubmed:issue |
40
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pubmed:dateCreated |
2003-9-29
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pubmed:databankReference |
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pubmed:abstractText |
The structure of the water-soluble, periplasmic domain of the fumarate sensor DcuS (DcuS-pd) has been determined by NMR spectroscopy in solution. DcuS is a prototype for a sensory histidine kinase with transmembrane signal transfer. DcuS belongs to the CitA family of sensors that are specific for sensing di- and tricarboxylates. The periplasmic domain is folded autonomously and shows helices at the N and the C terminus, suggesting direct linking or connection to helices in the two transmembrane regions. The structure constitutes a novel fold. The nearest structural neighbor is the Per-Arnt-Sim domain of the photoactive yellow protein that binds small molecules covalently. Residues Arg107, His110, and Arg147 are essential for fumarate sensing and are found clustered together. The structure constitutes the first periplasmic domain of a two component sensory system and is distinctly different from the aspartate sensory domain of the Tar chemotaxis sensor.
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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/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DcuS protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fumarates,
http://linkedlifedata.com/resource/pubmed/chemical/Histidine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Tar protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/fumaric acid
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
39185-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12907689-Amino Acid Sequence,
pubmed-meshheading:12907689-Arginine,
pubmed-meshheading:12907689-Bacterial Proteins,
pubmed-meshheading:12907689-Binding Sites,
pubmed-meshheading:12907689-Cell Membrane,
pubmed-meshheading:12907689-Chemoreceptor Cells,
pubmed-meshheading:12907689-Escherichia coli,
pubmed-meshheading:12907689-Escherichia coli Proteins,
pubmed-meshheading:12907689-Fumarates,
pubmed-meshheading:12907689-Histidine,
pubmed-meshheading:12907689-Magnetic Resonance Spectroscopy,
pubmed-meshheading:12907689-Models, Molecular,
pubmed-meshheading:12907689-Molecular Sequence Data,
pubmed-meshheading:12907689-Mutation,
pubmed-meshheading:12907689-Periplasm,
pubmed-meshheading:12907689-Protein Conformation,
pubmed-meshheading:12907689-Protein Folding,
pubmed-meshheading:12907689-Protein Kinases,
pubmed-meshheading:12907689-Protein Structure, Secondary,
pubmed-meshheading:12907689-Protein Structure, Tertiary,
pubmed-meshheading:12907689-Receptors, Cell Surface,
pubmed-meshheading:12907689-Signal Transduction
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pubmed:year |
2003
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pubmed:articleTitle |
The NMR structure of the sensory domain of the membranous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli.
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pubmed:affiliation |
Max Planck Institut für Biophysikalische Chemie, Am Fassberg 11, D-37077 Göttingen, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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