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Journal of Bacteriology, July 2006, p. 4970-4977, Vol. 188, No. 13
0021-9193/06/$08.00+0     doi:10.1128/JB.00160-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

The Crystal Structure of Beryllofluoride Spo0F in Complex with the Phosphotransferase Spo0B Represents a Phosphotransfer Pretransition State

Kottayil I. Varughese,1* Igor Tsigelny,2 and Haiyan Zhao1

Division of Cellular Biology, Department of Molecular and Experimental Medicine, MEM-116, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037,1 San Diego Supercomputer Center, University of California, San Diego, California 920932

Received 29 January 2006/ Accepted 10 April 2006

A number of regulatory circuits in biological systems function through the exchange of phosphoryl groups from one protein to another. Spo0F and Spo0B are components of a phosphorelay that control sporulation in the bacterium Bacillus subtilis through the exchange of a phosphoryl group. Using beryllofluoride as a mimic for phosphorylation, we trapped the interaction of the phosphorylated Spo0F with Spo0B in the crystal lattice. The transition state of phosphoryl transfer continues to be a highly debated issue, as to whether it is associative or dissociative in nature. The geometry of Spo0F binding to Spo0B favors an associative mechanism for phosphoryl transfer. In order to visualize the autophosphorylation of the histidine kinase, KinA, and the subsequent phosphoryl transfer to Spo0F, we generated in silico models representing these reaction steps.

* Corresponding author. Mailing address: Department of Molecular and Experimental Medicine, MEM-116, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037. Phone: (858) 784-7945. Fax: (858) 784-7966. E-mail: kiv{at}scripps.edu.

Journal of Bacteriology, July 2006, p. 4970-4977, Vol. 188, No. 13
0021-9193/06/$08.00+0     doi:10.1128/JB.00160-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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