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Structure paper

TitleArchitecture of the yeast Elongator complex.
Journal, issue, pagesEMBO Rep, Vol. 18, Issue 2, Page 264-279, Year 2017
Publish dateDec 14, 2016
AuthorsMaria I Dauden / Jan Kosinski / Olga Kolaj-Robin / Ambroise Desfosses / Alessandro Ori / Celine Faux / Niklas A Hoffmann / Osita F Onuma / Karin D Breunig / Martin Beck / Carsten Sachse / Bertrand Séraphin / Sebastian Glatt / Christoph W Müller /
PubMed AbstractThe 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 ...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.
External linksEMBO Rep / PubMed:27974378 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.812 - 31.0 Å
Structure data

EMDB-4151:
S.cerevisiae Elp123 sub-complex
Method: EM (single particle) / Resolution: 27.0 Å

EMDB-4152:
S.cerevisiae holoElongator complex
Method: EM (single particle) / Resolution: 31.0 Å

EMDB-4153:
S.cerevisiae partial Elp123 sub-complex
Method: EM (single particle) / Resolution: 31.0 Å

PDB-5m2n:
Crystal Structure of Elongator subunit Elp2
Method: X-RAY DIFFRACTION / Resolution: 2.812 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsRNA BINDING PROTEIN / Elongator / tRNA modifcation / Elp2 / WD40

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