Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 109, Issue 23, Pages E1481-E1488Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1200781109
Keywords
bacterial chemotaxis; protein-protein interactions; receptor clustering; signal transduction
Categories
Funding
- National Institute of Allergy and Infectious Diseases [R01AI087946]
- Welch Foundation [AU-1714]
- National Institute of General Medical Sciences [R01GM61074]
- Human Frontier Science Program
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The chemoreceptors of Escherichia coli localize to the cell poles and form a highly ordered array in concert with the CheA kinase and the CheW coupling factor. However, a high-resolution structure of the array has been lacking, and the molecular basis of array assembly has thus remained elusive. Here, we use cryoelectron tomography of flagellated E. coli minicells to derive a 3D map of the intact array. Docking of high-resolution structures into the 3D map provides a model of the core signaling complex, in which a CheA/CheW dimer bridges two adjacent receptor trimers via multiple hydrophobic interactions. A further, hitherto unknown, hydrophobic interaction between CheW and the homologous P5 domain of CheA in an adjacent core complex connects the complexes into an extended array. This architecture provides a structural basis for array formation and could explain the high sensitivity and cooperativity of chemotaxis signaling in E. coli.
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