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

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 solve...

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Bibliographic Details
Published in:The Journal of biological chemistry 2004-07, Vol.279 (27), p.28202-28208
Main Authors: Bae, Euiyoung, Phillips, Jr, George N
Format: Article
Language:English
Subjects:
Adenylate Kinase - chemistry
Amino Acid Sequence
Bacillus - enzymology
Bacillus globisporus
Bacillus stearothermophilus
Bacillus subtilis
Bacillus subtilis - enzymology
Calorimetry, Differential Scanning
Cloning, Molecular
Cold Temperature
Crystallography, X-Ray
Escherichia coli - metabolism
Geobacillus stearothermophilus - enzymology
Hot Temperature
Hydrogen Bonding
Models, Molecular
Molecular Sequence Data
Protein Conformation
Sequence Homology, Amino Acid
Species Specificity
Temperature
Zinc - chemistry
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M401865200