7SHQ
Structure of a functional construct of eukaryotic elongation factor 2 kinase in complex with calmodulin.
Summary for 7SHQ
| Entry DOI | 10.2210/pdb7shq/pdb |
| Descriptor | Eukaryotic elongation factor 2 kinase,Eukaryotic elongation factor 2 kinase, Calmodulin-1, ZINC ION, ... (6 entities in total) |
| Functional Keywords | elongation factor 2 kinase, eef2, calmodulin, translation |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 77369.17 |
| Authors | Piserchio, A.,Isiorho, E.A.,Jeruzalmi, D.,Dalby, K.N.,Ghose, R. (deposition date: 2021-10-11, release date: 2022-04-06, Last modification date: 2024-11-06) |
| Primary citation | Piserchio, A.,Isiorho, E.A.,Long, K.,Bohanon, A.L.,Kumar, E.A.,Will, N.,Jeruzalmi, D.,Dalby, K.N.,Ghose, R. Structural basis for the calmodulin-mediated activation of eukaryotic elongation factor 2 kinase. Sci Adv, 8:eabo2039-eabo2039, 2022 Cited by PubMed Abstract: Translation is a tightly regulated process that ensures optimal protein quality and enables adaptation to energy/nutrient availability. The α-kinase eukaryotic elongation factor 2 kinase (eEF-2K), a key regulator of translation, specifically phosphorylates the guanosine triphosphatase eEF-2, thereby reducing its affinity for the ribosome and suppressing the elongation phase of protein synthesis. eEF-2K activation requires calmodulin binding and autophosphorylation at the primary stimulatory site, T348. Biochemical studies predict a calmodulin-mediated activation mechanism for eEF-2K distinct from other calmodulin-dependent kinases. Here, we resolve the atomic details of this mechanism through a 2.3-Å crystal structure of the heterodimeric complex of calmodulin and the functional core of eEF-2K (eEF-2K). This structure, which represents the activated T348-phosphorylated state of eEF-2K, highlights an intimate association of the kinase with the calmodulin C-lobe, creating an "activation spine" that connects its amino-terminal calmodulin-targeting motif to its active site through a conserved regulatory element. PubMed: 35857468DOI: 10.1126/sciadv.abo2039 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.34 Å) |
Structure validation
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