Abstract
Coliform bacteria detect chemical attractants by means of a membrane-associated cluster of receptors and signalling molecules. We have used recently determined molecular structures, in conjunction with plastic models generated by three-dimensional printer technology, to predict how the proteins of the complex are arranged in relation to the plasma membrane. The proposed structure is a regular two-dimensional lattice in which the cytoplasmic ends of chemotactic-receptor dimers are inserted into a hexagonal array of CheA and CheW molecules. This structure creates separate compartments for adaptation and downstream signalling, and indicates a possible basis for the spread of activity within the cluster.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / chemistry*
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Bacterial Proteins / metabolism
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Chemotaxis / physiology*
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Escherichia coli / physiology*
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Escherichia coli Proteins*
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Histidine Kinase
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Membrane Proteins / chemistry*
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Membrane Proteins / metabolism
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Methyl-Accepting Chemotaxis Proteins
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Models, Molecular
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Protein Structure, Quaternary
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Receptors, Cell Surface / chemistry*
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Receptors, Cell Surface / metabolism
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Signal Transduction*
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Structure-Activity Relationship
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Thermotoga maritima / chemistry
Substances
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Bacterial Proteins
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CheW protein, E coli
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Escherichia coli Proteins
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Membrane Proteins
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Methyl-Accepting Chemotaxis Proteins
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Receptors, Cell Surface
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Tsr protein, Bacteria
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CheW protein, Bacteria
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Histidine Kinase
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cheA protein, E coli