This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Santelli, E.
Right arrow Articles by Szurmant, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Santelli, E.
Right arrow Articles by Szurmant, H.

 Previous Article  |  Next Article 

Journal of Bacteriology, April 2007, p. 3290-3295, Vol. 189, No. 8
0021-9193/07/$08.00+0     doi:10.1128/JB.01937-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

The Crystal Structure of Bacillus subtilis YycI Reveals a Common Fold for Two Members of an Unusual Class of Sensor Histidine Kinase Regulatory Proteins{triangledown} ,{dagger}

Eugenio Santelli,1 Robert C. Liddington,1 Michael A. Mohan,2 James A. Hoch,2* and Hendrik Szurmant2

Infectious and Inflammatory Disease Center, Burnham Institute for Medical Research, 10901 N. Torrey Pines Rd., La Jolla, California 92037,1 The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, California 920372

Received 21 December 2006/ Accepted 7 February 2007

YycI and YycH are two membrane-anchored periplasmic proteins that regulate the essential Bacillus subtilis YycG histidine kinase through direct interaction. Here we present the crystal structure of YycI at a 2.9-Å resolution. YycI forms a dimer, and remarkably the structure resembles that of the two C-terminal domains of YycH despite nearly undetectable sequence homology (10%) between the two proteins.

* Corresponding author. Mailing address: Division of Cellular Biology, Mail code MEM-116, Department of Molecular and Experimental Medicine, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037. Phone: (858) 784-7905. Fax: (858) 784-7966. E-mail: hoch{at}scripps.edu

{triangledown} Published ahead of print on 16 February 2007.

{dagger} Manuscript no. 18605 from The Scripps Research Institute.

Journal of Bacteriology, April 2007, p. 3290-3295, Vol. 189, No. 8
0021-9193/07/$08.00+0     doi:10.1128/JB.01937-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Szurmant, H., Bu, L., Brooks, C. L. III/, Hoch, J. A. (2008). An essential sensor histidine kinase controlled by transmembrane helix interactions with its auxiliary proteins. Proc. Natl. Acad. Sci. USA 105: 5891-5896 [Abstract] [Full Text]  
  • Szurmant, H., Mohan, M. A., Imus, P. M., Hoch, J. A. (2007). YycH and YycI Interact To Regulate the Essential YycFG Two-Component System in Bacillus subtilis. J. Bacteriol. 189: 3280-3289 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»