1P3J
Adenylate Kinase from Bacillus subtilis
Summary for 1P3J
| Entry DOI | 10.2210/pdb1p3j/pdb |
| Descriptor | Adenylate kinase, ZINC ION, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | zinc coordination, transferase |
| Biological source | Bacillus subtilis |
| Cellular location | Cytoplasm: P16304 |
| Total number of polymer chains | 1 |
| Total formula weight | 25153.48 |
| Authors | Bae, E.,Phillips Jr., G.N. (deposition date: 2003-04-17, release date: 2004-05-04, Last modification date: 2023-08-16) |
| Primary citation | Bae, E.,Phillips Jr., G.N. Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases. J.Biol.Chem., 279:28202-28208, 2004 Cited by PubMed Abstract: 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. PubMed: 15100224DOI: 10.1074/jbc.M401865200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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