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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.



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