1FOT
STRUCTURE OF THE UNLIGANDED CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT FROM SACCHAROMYCES CEREVISIAE
Summary for 1FOT
| Entry DOI | 10.2210/pdb1fot/pdb |
| Descriptor | CAMP-DEPENDENT PROTEIN KINASE TYPE 1 (2 entities in total) |
| Functional Keywords | camp-dependent protein kinase, open conformation, protein kinase, transferase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 37414.50 |
| Authors | Mashhoon, N.,Carmel, G.,Pflugrath, J.W.,Kuret, J. (deposition date: 2000-08-28, release date: 2001-06-13, Last modification date: 2024-10-09) |
| Primary citation | Mashhoon, N.,Carmel, G.,Pflugrath, J.W.,Kuret, J. Structure of the unliganded cAMP-dependent protein kinase catalytic subunit from Saccharomyces cerevisiae. Arch.Biochem.Biophys., 387:11-19, 2001 Cited by PubMed Abstract: The structure of TPK1delta, a truncated variant of the cAMP-dependent protein kinase catalytic subunit from Saccharomyces cerevisiae, was determined in an unliganded state at 2.8 A resolution and refined to a crystallographic R-factor of 19.4%. Comparison of this structure to that of its fully liganded mammalian homolog revealed a highly conserved protein fold comprised of two globular lobes. Within each lobe, root mean square deviations in Calpha positions averaged approximately equals 0.9 A. In addition, a phosphothreonine residue was found in the C-terminal domain of each enzyme. Further comparison of the two structures suggests that a trio of conformational changes accompanies ligand-binding. The first consists of a 14.7 degrees rigid-body rotation of one lobe relative to the other and results in closure of the active site cleft. The second affects only the glycine-rich nucleotide binding loop, which moves approximately equals 3 A to further close the active site and traps the nucleotide substrate. The third is localized to a C-terminal segment that makes direct contact with ligands and the ligand-binding cleft. In addition to resolving the conformation of unliganded enzyme, the model shows that the salient features of the cAMP-dependent protein kinase are conserved over long evolutionary distances. PubMed: 11368172DOI: 10.1006/abbi.2000.2241 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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