3O7L
Crystal Structure of phospholamban (1-19):PKA C-subunit:AMP-PNP:Mg2+ complex
Summary for 3O7L
| Entry DOI | 10.2210/pdb3o7l/pdb |
| Related | 1ATP |
| Descriptor | cAMP-dependent protein kinase catalytic subunit alpha, Cardiac phospholamban, MAGNESIUM ION, ... (7 entities in total) |
| Functional Keywords | protein kinase a, phospholamban, allostery, substrate recognition, conformational selection, intrinsically disordered proteins, membrane proteins, transferase |
| Biological source | Mus musculus (mouse) More |
| Cellular location | Cytoplasm (By similarity): P05132 P05132 Mitochondrion membrane; Single-pass membrane protein: P61014 |
| Total number of polymer chains | 3 |
| Total formula weight | 83633.60 |
| Authors | Cheng, C.Y.,Taylor, S.S. (deposition date: 2010-07-30, release date: 2010-10-06, Last modification date: 2024-10-16) |
| Primary citation | Masterson, L.R.,Cheng, C.,Yu, T.,Tonelli, M.,Kornev, A.,Taylor, S.S.,Veglia, G. Dynamics connect substrate recognition to catalysis in protein kinase A. Nat.Chem.Biol., 6:821-828, 2010 Cited by PubMed Abstract: Atomic resolution studies of protein kinases have traditionally been carried out in the inhibitory state, limiting our current knowledge on the mechanisms of substrate recognition and catalysis. Using NMR, X-ray crystallography and thermodynamic measurements, we analyzed the substrate recognition process of cAMP-dependent protein kinase (PKA), finding that entropy and protein dynamics play a prominent role. The nucleotide acts as a dynamic and allosteric activator by coupling the two lobes of apo PKA, enhancing the enzyme dynamics synchronously and priming it for catalysis. The formation of the ternary complex is entropically driven, and NMR spin relaxation data reveal that both substrate and PKA are dynamic in the closed state. Our results show that the enzyme toggles between open and closed states, which indicates that a conformational selection rather than an induced-fit mechanism governs substrate recognition. PubMed: 20890288DOI: 10.1038/nchembio.452 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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