Structural Analysis of Staphylococcus aureus Serine/Threonine Kinase PknB
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- Effective treatment of infections caused by the bacterium Staphylococcus aureus remains a worldwide challenge, in part due to the constant emergence of new strains that are resistant to antibiotics. The serine/threonine kinase PknB is of particular relevance to the life cycle of S. aureus as it is involved in the regulation of purine biosynthesis, autolysis, and other central metabolic processes of the bacterium. We have determined the crystal structure of the kinase domain of PknB in complex with a non-hydrolyzable analog of the substrate ATPEffective treatment of infections caused by the bacterium Staphylococcus aureus remains a worldwide challenge, in part due to the constant emergence of new strains that are resistant to antibiotics. The serine/threonine kinase PknB is of particular relevance to the life cycle of S. aureus as it is involved in the regulation of purine biosynthesis, autolysis, and other central metabolic processes of the bacterium. We have determined the crystal structure of the kinase domain of PknB in complex with a non-hydrolyzable analog of the substrate ATP at 3.0 angstrom resolution. Although the purified PknB kinase is active in solution, it crystallized in an inactive, autoinhibited state. Comparison with other bacterial kinases provides insights into the determinants of catalysis, interactions of PknB with ligands, and the pathway of activation.…
Autor(en): | Sonja Rakette, Stefanie Donat, Knut Ohlsen, Thilo Stehle |
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URN: | urn:nbn:de:bvb:20-opus-135369 |
Dokumentart: | Artikel / Aufsatz in einer Zeitschrift |
Institute der Universität: | Medizinische Fakultät / Institut für Molekulare Infektionsbiologie |
Sprache der Veröffentlichung: | Englisch |
Titel des übergeordneten Werkes / der Zeitschrift (Englisch): | PLoS One |
Erscheinungsjahr: | 2012 |
Band / Jahrgang: | 7 |
Heft / Ausgabe: | 6 |
Seitenangabe: | e39136 |
Originalveröffentlichung / Quelle: | PLoS ONE 7(6): e39136. doi:10.1371/journal.pone.0039136 |
DOI: | https://doi.org/10.1371/journal.pone.0039136 |
Allgemeine fachliche Zuordnung (DDC-Klassifikation): | 6 Technik, Medizin, angewandte Wissenschaften / 61 Medizin und Gesundheit / 610 Medizin und Gesundheit |
Freie Schlagwort(e): | SER/THR kinase; activation mechanism; antibiotic resistance; catalytic; crystal structure; dependent protein-kinase; domain; inhibitor; methicillin; mycobacterium-tuberculosis; subunit |
Datum der Freischaltung: | 23.03.2018 |
Lizenz (Deutsch): | CC BY: Creative-Commons-Lizenz: Namensnennung |