Zinc, a novel structural element found in the family of bacterial adenylate kinases
| Autor: | Muriel Delepierre, Henry H. Mantsch, Octavian Barzu, Anne-Marie Gilles, Witold K. Surewicz, Philippe Glaser, Elena Presecan |
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| Přispěvatelé: | Régulation de l'Expression Génétique (REG), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Biochimie des Régulations Cellulaires, Résonance Magnétique Nucléaire, Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur [Paris], Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 1992 |
| Předmět: |
inorganic chemicals
[SDV]Life Sciences [q-bio] Genetic Vectors Molecular Sequence Data Adenylate kinase lac operon Bacillus subtilis medicine.disease_cause Biochemistry Geobacillus stearothermophilus Structure-Activity Relationship 03 medical and health sciences Bacterial Proteins Enzyme Stability medicine heterocyclic compounds Amino Acid Sequence Cloning Molecular Escherichia coli 030304 developmental biology 0303 health sciences Base Sequence biology Kinase Adenylate Kinase fungi 030302 biochemistry & molecular biology Lactococcus lactis Protein primary structure biology.organism_classification ADK Kinetics Zinc Genes Bacterial Multigene Family Thermodynamics bacteria Protein Binding |
| Zdroj: | biochemistry (Moscow) biochemistry (Moscow), 1992, 31, pp.3038-3043. ⟨10.1021/bi00127a002⟩ |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi00127a002 |
| Popis: | The adk gene from Bacillus stearothermophilus was cloned and overexpressed in Escherichia coli under the control of the lac promoter. The primary structure of B. stearothermophilus adenylate kinase exhibited 76% identity with the enzyme from Bacillus subtilis, 60% identity with the enzyme from Lactococcus lactis, and 42% identity with the enzyme from E. coli. The most striking property of the adenylate kinase from B. stearothermophilus is the presence of a structural zinc atom bound to four cysteines in a zinc finger-like fashion. The ability to coordinate zinc is predicted also for a number of other isoforms of bacterial adenylate kinases. Furthermore, the tightly bound metal ion contributes to the high thermodynamic stability of adenylate kinase from B. stearothermophilus. |
| Databáze: | OpenAIRE |
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