1p3j
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(New page: 200px<br /><applet load="1p3j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p3j, resolution 1.90Å" /> '''Adenylate Kinase fro...)
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Revision as of 21:19, 20 November 2007
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Adenylate Kinase from Bacillus subtilis
Overview
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.
About this Structure
1P3J is a Single protein structure of sequence from Bacillus subtilis with ZN, MG and AP5 as ligands. Active as Adenylate kinase, with EC number 2.7.4.3 Full crystallographic information is available from OCA.
Reference
Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases., Bae E, Phillips GN Jr, J Biol Chem. 2004 Jul 2;279(27):28202-8. Epub 2004 Apr 20. PMID:15100224
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