Molecular model of a lattice of signalling proteins involved in bacterial chemotaxis

Nat Cell Biol. 2000 Nov;2(11):792-6. doi: 10.1038/35041030.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Chemotaxis / physiology*
  • Escherichia coli / physiology*
  • Escherichia coli Proteins*
  • Histidine Kinase
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism
  • Methyl-Accepting Chemotaxis Proteins
  • Models, Molecular
  • Protein Structure, Quaternary
  • Receptors, Cell Surface / chemistry*
  • Receptors, Cell Surface / metabolism
  • Signal Transduction*
  • Structure-Activity Relationship
  • Thermotoga maritima / chemistry

Substances

  • Bacterial Proteins
  • CheW protein, E coli
  • Escherichia coli Proteins
  • Membrane Proteins
  • Methyl-Accepting Chemotaxis Proteins
  • Receptors, Cell Surface
  • Tsr protein, Bacteria
  • CheW protein, Bacteria
  • Histidine Kinase
  • cheA protein, E coli