Molecular architecture of chemoreceptor arrays revealed by cryoelectron tomography of Escherichia coli minicells
| Autor: | Michael D. Manson, Sneha Jani, William Margolin, Bo Hu, Jun Liu, Dustin R. Morado |
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| Rok vydání: | 2012 |
| Předmět: |
Models
Molecular Electron Microscope Tomography Histidine Kinase Molecular Conformation Methyl-Accepting Chemotaxis Proteins Cooperativity Biology medicine.disease_cause Protein–protein interaction Bacterial Proteins Escherichia coli medicine Multidisciplinary Methyl-accepting chemotaxis protein Chemotaxis Escherichia coli Proteins Cryoelectron Microscopy Histidine kinase Membrane Proteins PNAS Plus Biochemistry Docking (molecular) Biophysics Receptor clustering Dimerization Signal Transduction |
| Zdroj: | Proceedings of the National Academy of Sciences. 109 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.1200781109 |
| Popis: | 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 . |
| Databáze: | OpenAIRE |
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