Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Cryo-EM structure of the fully assembled Elongator complex.
Journal, issue, pages	Nucleic Acids Res, Vol. 51, Issue 5, Page 2011-2032, Year 2023
Publish date	Mar 21, 2023
Authors	Marcin Jaciuk / David Scherf / Karol Kaszuba / Monika Gaik / Alexander Rau / Anna Kościelniak / Rościsław Krutyhołowa / Michał Rawski / Paulina Indyka / Andrea Graziadei / Andrzej Chramiec-Głąbik / Anna Biela / Dominika Dobosz / Ting-Yu Lin / Nour-El-Hana Abbassi / Alexander Hammermeister / Juri Rappsilber / Jan Kosinski / Raffael Schaffrath / Sebastian Glatt /
PubMed Abstract	Transfer RNA (tRNA) molecules are essential to decode messenger RNA codons during protein synthesis. All known tRNAs are heavily modified at multiple positions through post-transcriptional addition ...Transfer RNA (tRNA) molecules are essential to decode messenger RNA codons during protein synthesis. All known tRNAs are heavily modified at multiple positions through post-transcriptional addition of chemical groups. Modifications in the tRNA anticodons are directly influencing ribosome decoding and dynamics during translation elongation and are crucial for maintaining proteome integrity. In eukaryotes, wobble uridines are modified by Elongator, a large and highly conserved macromolecular complex. Elongator consists of two subcomplexes, namely Elp123 containing the enzymatically active Elp3 subunit and the associated Elp456 hetero-hexamer. The structure of the fully assembled complex and the function of the Elp456 subcomplex have remained elusive. Here, we show the cryo-electron microscopy structure of yeast Elongator at an overall resolution of 4.3 Å. We validate the obtained structure by complementary mutational analyses in vitro and in vivo. In addition, we determined various structures of the murine Elongator complex, including the fully assembled mouse Elongator complex at 5.9 Å resolution. Our results confirm the structural conservation of Elongator and its intermediates among eukaryotes. Furthermore, we complement our analyses with the biochemical characterization of the assembled human Elongator. Our results provide the molecular basis for the assembly of Elongator and its tRNA modification activity in eukaryotes.
External links	Nucleic Acids Res / PubMed:36617428 / PubMed Central
Methods	EM (single particle)
Resolution	3.7 - 5.92 Å
Structure data	15622 8asv EMDB-15622, PDB-8asv: Cryo-EM structure of yeast Elongator complex Method: EM (single particle) / Resolution: 4.35 Å 15623 8asw EMDB-15623, PDB-8asw: Cryo-EM structure of yeast Elp123 in complex with alanine tRNA Method: EM (single particle) / Resolution: 3.96 Å EMDB-15625: Cryo-EM structure of mouse Elp123 in complex with alanine tRNA Method: EM (single particle) / Resolution: 4.35 Å EMDB-15626: Cryo-EM structure of mouse Elongator complex Method: EM (single particle) / Resolution: 5.92 Å 15635 8at6 EMDB-15635, PDB-8at6: Cryo-EM structure of yeast Elp456 subcomplex Method: EM (single particle) / Resolution: 3.7 Å 15682 8avg EMDB-15682, PDB-8avg: Cryo-EM structure of mouse Elp123 with bound SAM Method: EM (single particle) / Resolution: 4.01 Å
Chemicals	ChemComp-SF4: IRON/SULFUR CLUSTER / Iron–sulfur cluster ChemComp-5AD: 5'-DEOXYADENOSINE / Deoxyadenosine ChemComp-SAM: S-ADENOSYLMETHIONINE / S-Adenosyl methionine
Source	saccharomyces cerevisiae (brewer's yeast) mus musculus (house mouse)
Keywords	TRANSLATION / wobble uridine modification