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J. Biol. Chem., Vol. 279, Issue 27, 28202-28208, July 2, 2004

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Structures and Analysis of Highly Homologous Psychrophilic, Mesophilic, and Thermophilic Adenylate Kinases^*

Euiyoung Bae and George N. Phillips, Jr.

From the Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706

The crystal structures of adenylate kinases from the psychrophile Bacillus globisporus and the mesophile Bacillus subtilis have been solved and compared with that from the thermophile Bacillus stearothermophilus. This is the first example we know of where a trio of protein structures has been solved that have the same number of amino acids and a high level of identity (66–74%) and yet come from organisms with different operating temperatures. The enzymes were characterized for their own thermal denaturation and inactivation, and they exhibited the same temperature preferences as their source organisms. The structures of the three highly homologous, dynamic proteins with different temperature-activity profiles provide an opportunity to explore a molecular mechanism of cold and heat adaptation. Their analysis suggests that the maintenance of the balance between stability and flexibility is crucial for proteins to function at their environmental temperatures, and it is achieved by the modification of intramolecular interactions in the process of temperature adaptation.

Received for publication, February 20, 2004 , and in revised form, April 19, 2004.

^* This work was supported by a Vilas Associate Award (to G. N. P.) and the Wisconsin Alumni Research Foundation. Use of the Advanced Photon Source was supported by the United States Department of Energy, Basic Energy Sciences, Office of Science under Contract W-31-109-Eng-38. Use of the BioCARS beamline was supported by the National Institutes of Health, National Center for Research Resources under Grant number RR07707. Use of the Biophysics Instrumentation Facility was supported by the University of Wisconsin-Madison, National Science Foundation Grant BIR-9512577, and National Institutes of Health Grant S10 RR13790. 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.

The atomic coordinates and structure factors (codes 1S3G and 1P3J) 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: Dept. of Biochemistry, University of Wisconsin, 433 Babcock Dr., Madison, WI 53706. Tel.: 608-263-6142; Fax: 608-262-3453; E-mail: phillips{at}biochem.wisc.edu.

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