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Originally published In Press as doi:10.1074/jbc.C100295200 on June 15, 2001

J. Biol. Chem., Vol. 276, Issue 31, 28637-28640, August 3, 2001
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ACCELERATED PUBLICATION
A Distinct Meta-active Conformation in the 1.1-Å Resolution Structure of Wild-type ApoCheY*

Miljan SimonovicDagger and Karl Volz§

From the Departments of Dagger  Biochemistry and Molecular Biology and § Microbiology and Immunology, University of Illinois at Chicago, Chicago, Illinois 60612-7334

CheY is the best characterized member of the response regulator superfamily, and as such it has become the principal model for understanding the initial molecular mechanisms of signaling in two-component systems. Normal signaling by response regulators requires phosphorylation, in combination with an activation mechanism whose conformational effects are not completely understood. CheY activation involves three events, phosphorylation, a conformational change in the beta 4-alpha 4 loop, and a rotational restriction of the side chain of tyrosine 106. An outstanding question concerns the nature of an active conformation in the apoCheY population. The details of this 1.08-Å resolution crystal structure of wild-type apoCheY shows the beta 4-alpha 4 loop in two distinctly different conformations that sterically correlate with the two rotameric positions of the tyrosine 106 side chain. One of these conformational states of CheY is the inactive form, and we propose that the other is a meta-active form, responsible for the active properties seen in apoCheY.

* This work was supported in part by National Institutes of Health Grant GM47522 (to K. V.) and by funds from the Vice Chancellor for Research, University of Illinois at Chicago (to M. S.). M. S. is the recipient of a University Fellowship from the University of Illinois at Chicago.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and the structure factors (code 1JBE) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

To whom correspondence should be addressed. Tel.: 312-996-2314; Fax: 312-355-4535; E-mail: kvolz@uic.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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