Originally published In Press as doi:10.1074/jbc.M400077200 on March 8, 2004
J. Biol. Chem., Vol. 279, Issue 19, 20511-20518, May 7, 2004
Crystal Structure of Circadian Clock Protein KaiA from Synechococcus elongatus*
Sheng Ye
,
Ioannis Vakonakis¶,
Thomas R. Ioerger||,
Andy C. LiWang¶**, and
James C. Sacchettini¶**
From the
Center for Structural Biology, Institute of Biosciences and Technology, Houston, Texas 77030, the ¶Department of Biochemistry and Biophysics, Center for Structural Biology, Texas A&M, University, College Station, Texas 77843-2128, and the ||Department of Computer Science, Texas A & M University, College Station, Texas 77843-2128
The circadian clock found in Synechococcus elongatus, the most ancient circadian clock, is regulated by the interaction of three proteins, KaiA, KaiB, and KaiC. While the precise function of these proteins remains unclear, KaiA has been shown to be a positive regulator of the expression of KaiB and KaiC. The 2.0-Å structure of KaiA of S. elongatus reported here shows that the protein is composed of two independently folded domains connected by a linker. The NH2-terminal pseudo-receiver domain has a similar fold with that of bacterial response regulators, whereas the COOH-terminal four-helix bundle domain is novel and forms the interface of the 2-fold-related homodimer. The COOH-terminal four-helix bundle domain has been shown to contain the KaiC binding site. The structure suggests that the KaiB binding site is covered in the dimer interface of the KaiA "closed" conformation, observed in the crystal structure, which suggests an allosteric regulation mechanism.
Received for publication, January 5, 2004
, and in revised form, March 1, 2004.
The atomic coordinates and structure factors (code 1R8J) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).
* This work was supported by the Robert A. Welch Foundation (to J. C. S.) and National Institutes of Health Grants GM064576 (to A. C. L.) and GM62410 (to J. C. S.). Use of the Argonne National Laboratory Structural Biology Center beamlines at the Advanced Photon Source was supported by the United States Department of Energy Office of Energy Research under contract number W-31-109-ENG-38. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
These authors contributed equally to this work.
** To whom correspondence may be addressed: Dept. of Biochemistry and Biophysics, Center for Structural Biology, Texas A & M, University, College Station, TX 77843-2128. E-mail: andy-liwang{at}tamu.edu (for A. C. L.) or sacchett{at}tamu.edu (for J. C. S.).
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Copyright © 2004 by the American Society for Biochemistry and Molecular Biology.
