4EQM
Structural analysis of Staphylococcus aureus serine/threonine kinase PknB
Summary for 4EQM
| Entry DOI | 10.2210/pdb4eqm/pdb |
| Descriptor | Protein kinase, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, BENZAMIDINE (3 entities in total) |
| Functional Keywords | kinase, serine/threonine protein kinase, transferase |
| Biological source | Staphylococcus aureus subsp. aureus |
| Total number of polymer chains | 6 |
| Total formula weight | 202312.87 |
| Authors | Rakette, S.,Stehle, T. (deposition date: 2012-04-19, release date: 2012-06-27, Last modification date: 2024-02-28) |
| Primary citation | Rakette, S.,Donat, S.,Ohlsen, K.,Stehle, T. Structural Analysis of Staphylococcus aureus Serine/Threonine Kinase PknB. Plos One, 7:e39136-e39136, 2012 Cited by PubMed Abstract: 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 ATP at 3.0 Å 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. PubMed: 22701750DOI: 10.1371/journal.pone.0039136 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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