Conformational Coupling between Receptor and Kinase Binding Sites through a Conserved Salt Bridge in a Signaling Complex Scaffold Protein
Abstract
Bacterial chemotaxis is one of the best studied signal transduction pathways. CheW is a scaffold protein that mediates the association of the chemoreceptors and the CheA kinase in a ternary signaling complex. The effects of replacing conserved Arg62 of CheW with other residues suggested that the scaffold protein plays a more complex role than simply binding its partner proteins. Although R62A CheW had essentially the same affinity for chemoreceptors and CheA, cells expressing the mutant protein are impaired in chemotaxis. Using a combination of molecular dynamics simulations (MD), NMR spectroscopy, and circular dichroism (CD), we addressed the role of Arg62. Here we show that Arg62 forms a salt bridge with another highly conserved residue, Glu38. Although this interaction is unimportant for overall protein stability, it is essential to maintain the correct alignment of the chemoreceptor and kinase binding sites of CheW. Computational and experimental data suggest that the role of the salt bridge in maintaining the alignment of the two partner binding sites is fundamental to the function of the signaling complex but not to its assembly. We conclude that a key feature of CheW is to maintain the specific geometry between the two interaction sites required for its functionmore »
- Authors:
-
- Univ. of Tennessee, Knoxville, TN (United States). Joint Inst. for Computational Sciences; Univ. of Tennessee, Knoxville, TN (United States). Dept. of Physics
- Univ. of California, Santa Barbara, CA (United States). Dept. of Chemistry and Biochemistry
- Univ. of Tennessee, Knoxville, TN (United States). Dept. Biochemistry and Cell and Molecular Biology; Univ. of Tennessee, Knoxville, TN (United States). Center for Molecular Biophysics
- Univ. of Tennessee, Knoxville, TN (United States). Joint Inst. for Computational Sciences; Univ. of Tennessee, Knoxville, TN (United States). Dept. of Microbiology
- Publication Date:
- Research Org.:
- Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division; National Institutes of Health (NIH)
- OSTI Identifier:
- 1627232
- Grant/Contract Number:
- AC05-00OR22725; GM07225; GM059544
- Resource Type:
- Accepted Manuscript
- Journal Name:
- PLoS Computational Biology (Online)
- Additional Journal Information:
- Journal Name: PLoS Computational Biology (Online); Journal Volume: 9; Journal Issue: 11; Journal ID: ISSN 1553-7358
- Publisher:
- Public Library of Science
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; Biochemistry & Molecular Biology; Mathematical & Computational Biology
Citation Formats
Ortega, Davi R., Mo, Guoya, Lee, Kwangwoon, Zhou, Hongjun, Baudry, Jerome, Dahlquist, Frederick W., and Zhulin, Igor B. Conformational Coupling between Receptor and Kinase Binding Sites through a Conserved Salt Bridge in a Signaling Complex Scaffold Protein. United States: N. p., 2013.
Web. doi:10.1371/journal.pcbi.1003337.
Ortega, Davi R., Mo, Guoya, Lee, Kwangwoon, Zhou, Hongjun, Baudry, Jerome, Dahlquist, Frederick W., & Zhulin, Igor B. Conformational Coupling between Receptor and Kinase Binding Sites through a Conserved Salt Bridge in a Signaling Complex Scaffold Protein. United States. https://doi.org/10.1371/journal.pcbi.1003337
Ortega, Davi R., Mo, Guoya, Lee, Kwangwoon, Zhou, Hongjun, Baudry, Jerome, Dahlquist, Frederick W., and Zhulin, Igor B. Thu .
"Conformational Coupling between Receptor and Kinase Binding Sites through a Conserved Salt Bridge in a Signaling Complex Scaffold Protein". United States. https://doi.org/10.1371/journal.pcbi.1003337. https://www.osti.gov/servlets/purl/1627232.
@article{osti_1627232,
title = {Conformational Coupling between Receptor and Kinase Binding Sites through a Conserved Salt Bridge in a Signaling Complex Scaffold Protein},
author = {Ortega, Davi R. and Mo, Guoya and Lee, Kwangwoon and Zhou, Hongjun and Baudry, Jerome and Dahlquist, Frederick W. and Zhulin, Igor B.},
abstractNote = {Bacterial chemotaxis is one of the best studied signal transduction pathways. CheW is a scaffold protein that mediates the association of the chemoreceptors and the CheA kinase in a ternary signaling complex. The effects of replacing conserved Arg62 of CheW with other residues suggested that the scaffold protein plays a more complex role than simply binding its partner proteins. Although R62A CheW had essentially the same affinity for chemoreceptors and CheA, cells expressing the mutant protein are impaired in chemotaxis. Using a combination of molecular dynamics simulations (MD), NMR spectroscopy, and circular dichroism (CD), we addressed the role of Arg62. Here we show that Arg62 forms a salt bridge with another highly conserved residue, Glu38. Although this interaction is unimportant for overall protein stability, it is essential to maintain the correct alignment of the chemoreceptor and kinase binding sites of CheW. Computational and experimental data suggest that the role of the salt bridge in maintaining the alignment of the two partner binding sites is fundamental to the function of the signaling complex but not to its assembly. We conclude that a key feature of CheW is to maintain the specific geometry between the two interaction sites required for its function as a scaffold.},
doi = {10.1371/journal.pcbi.1003337},
journal = {PLoS Computational Biology (Online)},
number = 11,
volume = 9,
place = {United States},
year = {Thu Nov 14 00:00:00 EST 2013},
month = {Thu Nov 14 00:00:00 EST 2013}
}
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