6NX4
Structure of the C-terminal Helical Repeat Domain of Eukaryotic Elongation Factor 2 Kinase (eEF-2K)
Summary for 6NX4
| Entry DOI | 10.2210/pdb6nx4/pdb |
| NMR Information | BMRB: 30569 |
| Descriptor | Eukaryotic elongation factor 2 kinase (1 entity in total) |
| Functional Keywords | eef2k, eef2, binding domain, kinase, transferase, sel1, elongation, tpr, translation |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 18893.02 |
| Authors | Piserchio, A.,Will, N.,Giles, D.H.,Hajredini, F.,Dalby, K.N.,Ghose, R. (deposition date: 2019-02-08, release date: 2019-05-29, Last modification date: 2024-05-01) |
| Primary citation | Piserchio, A.,Will, N.,Giles, D.H.,Hajredini, F.,Dalby, K.N.,Ghose, R. Solution Structure of the Carboxy-Terminal Tandem Repeat Domain of Eukaryotic Elongation Factor 2 Kinase and Its Role in Substrate Recognition. J.Mol.Biol., 431:2700-2717, 2019 Cited by PubMed Abstract: Eukaryotic elongation factor 2 kinase (eEF-2K), an atypical calmodulin-activated protein kinase, regulates translational elongation by phosphorylating its substrate, eukaryotic elongation factor 2 (eEF-2), thereby reducing its affinity for the ribosome. The activation and activity of eEF-2K are critical for survival under energy-deprived conditions and is implicated in a variety of essential physiological processes. Previous biochemical experiments have indicated that the binding site for the substrate eEF-2 is located in the C-terminal domain of eEF-2K, a region predicted to harbor several α-helical repeats. Here, using NMR methodology, we have determined the solution structure of a C-terminal fragment of eEF-2K, eEF-2K that encodes two α-helical repeats. The structure of eEF-2K shows signatures characteristic of TPR domains and of their SEL1-like sub-family. Furthermore, using the analyses of NMR spectral perturbations and ITC measurements, we have localized the eEF-2 binding site on eEF-2K. We find that eEF-2K engages eEF-2 with an affinity comparable to that of the full-length enzyme. Furthermore, eEF-2K is able to inhibit the phosphorylation of eEF-2 by full-length eEF-2K in trans. Our present studies establish that eEF-2K encodes the major elements necessary to enable the eEF-2K/eEF-2 interactions. PubMed: 31108082DOI: 10.1016/j.jmb.2019.05.019 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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