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| {{STRUCTURE_1p3j| PDB=1p3j | SCENE= }} | | {{STRUCTURE_1p3j| PDB=1p3j | SCENE= }} |
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| '''Adenylate Kinase from Bacillus subtilis'''
| | ===Adenylate Kinase from Bacillus subtilis=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_15100224}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15100224 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15100224}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Jr., G N.Phillips.]] | | [[Category: Jr., G N.Phillips.]] |
| [[Category: Zinc coordination]] | | [[Category: Zinc coordination]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:38:24 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:28:54 2008'' |
