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Journal of Bacteriology, September 2009, p. 5845-5848, Vol. 191, No. 18
0021-9193/09/$08.00+0     doi:10.1128/JB.00294-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

The CheZ Binding Interface of CheAS Is Located in {alpha}-Helix E{triangledown}

Christopher O'Connor,{dagger} Philip Matsumura, and Andres Campos*

Department of Microbiology and Immunology, College of Medicine, University of Illinois at Chicago, Chicago, Illinois 60612

Received 4 March 2009/ Accepted 29 June 2009

Specific CheA-short (CheAS) residues, L123 and L126, were identified as critical for CheZ binding. In the CheAS 'P1-CheZ nuclear magnetic resonance structure, these residues form an interaction surface on {alpha}-helix E in the 'P1 domain. Both L123 and L126 are buried in CheA-long (CheAL), providing an explanation for why CheAL fails to bind CheZ.

* Corresponding author. Mailing address: Molecular Biology Consortium, 835 S. Wolcott Ave. (M/C 790), MSB E-603, Chicago, IL 60612-7344. Phone: (312) 996-1216. Fax: (312) 413-2952. E-mail: acampos{at}uic.edu

{triangledown} Published ahead of print on 6 July 2009.

{dagger} Present address: Department of Cell Biology, Neurology and Anatomy, Loyola University Medical School, 2160 South First Ave., Bldg. 102, Maywood, IL 60153.

Journal of Bacteriology, September 2009, p. 5845-5848, Vol. 191, No. 18
0021-9193/09/$08.00+0     doi:10.1128/JB.00294-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Cantwell, B. J., Manson, M. D. (2009). Protein Domains and Residues Involved in the CheZ/CheAS Interaction. J. Bacteriol. 191: 5838-5841 [Abstract] [Full Text]  


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