5M2N
Crystal Structure of Elongator subunit Elp2
Summary for 5M2N
| Entry DOI | 10.2210/pdb5m2n/pdb |
| Related | 4XFV |
| Descriptor | Elongator complex protein 2 (2 entities in total) |
| Functional Keywords | elongator, trna modifcation, elp2, wd40, rna binding protein |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Cellular location | Cytoplasm: P42935 |
| Total number of polymer chains | 1 |
| Total formula weight | 90129.08 |
| Authors | Glatt, S.,Mueller, C.W. (deposition date: 2016-10-13, release date: 2016-12-28, Last modification date: 2024-11-13) |
| Primary citation | Dauden, M.I.,Kosinski, J.,Kolaj-Robin, O.,Desfosses, A.,Ori, A.,Faux, C.,Hoffmann, N.A.,Onuma, O.F.,Breunig, K.D.,Beck, M.,Sachse, C.,Seraphin, B.,Glatt, S.,Muller, C.W. Architecture of the yeast Elongator complex. EMBO Rep., 18:264-279, 2017 Cited by PubMed Abstract: The highly conserved eukaryotic Elongator complex performs specific chemical modifications on wobble base uridines of tRNAs, which are essential for proteome stability and homeostasis. The complex is formed by six individual subunits (Elp1-6) that are all equally important for its tRNA modification activity. However, its overall architecture and the detailed reaction mechanism remain elusive. Here, we report the structures of the fully assembled yeast Elongator and the Elp123 sub-complex solved by an integrative structure determination approach showing that two copies of the Elp1, Elp2, and Elp3 subunits form a two-lobed scaffold, which binds Elp456 asymmetrically. Our topological models are consistent with previous studies on individual subunits and further validated by complementary biochemical analyses. Our study provides a structural framework on how the tRNA modification activity is carried out by Elongator. PubMed: 27974378DOI: 10.15252/embr.201643353 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.812 Å) |
Structure validation
Download full validation report
