4O22
Binary complex of metal-free PKAc with SP20.
Summary for 4O22
| Entry DOI | 10.2210/pdb4o22/pdb |
| Related | 4O21 |
| Descriptor | cAMP-dependent protein kinase catalytic subunit alpha., Phosphorylated peptide pSP20. (3 entities in total) |
| Functional Keywords | ser/thr kinase, phosphoryl transfer, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Mus musculus (mouse) More |
| Cellular location | Cytoplasm. Isoform 2: Cell projection, cilium, flagellum (By similarity): P05132 |
| Total number of polymer chains | 2 |
| Total formula weight | 42434.17 |
| Authors | Das, A.,Kovalevsky, A.Y.,Gerlits, O.,Langan, P.,Heller, W.T.,Keshwani, M.,Taylor, S.S. (deposition date: 2013-12-16, release date: 2014-05-28, Last modification date: 2024-11-06) |
| Primary citation | Gerlits, O.,Das, A.,Keshwani, M.M.,Taylor, S.,Waltman, M.J.,Langan, P.,Heller, W.T.,Kovalevsky, A. Metal-Free cAMP-Dependent Protein Kinase Can Catalyze Phosphoryl Transfer. Biochemistry, 53:3179-3186, 2014 Cited by PubMed Abstract: X-ray structures of several ternary product complexes of the catalytic subunit of cAMP-dependent protein kinase (PKAc) have been determined with no bound metal ions and with Na(+) or K(+) coordinated at two metal-binding sites. The metal-free PKAc and the enzyme with alkali metals were able to facilitate the phosphoryl transfer reaction. In all studied complexes, the ATP and the substrate peptide (SP20) were modified into the products ADP and the phosphorylated peptide. The products of the phosphotransfer reaction were also found when ATP-γS, a nonhydrolyzable ATP analogue, reacted with SP20 in the PKAc active site containing no metals. Single turnover enzyme kinetics measurements utilizing (32)P-labeled ATP confirmed the phosphotransferase activity of the enzyme in the absence of metal ions and in the presence of alkali metals. In addition, the structure of the apo-PKAc binary complex with SP20 suggests that the sequence of binding events may become ordered in a metal-free environment, with SP20 binding first to prime the enzyme for subsequent ATP binding. Comparison of these structures reveals conformational and hydrogen bonding changes that might be important for the mechanism of catalysis. PubMed: 24786636DOI: 10.1021/bi5000965 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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