6QK7

Elongator catalytic subcomplex Elp123 lobe

Summary for 6QK7

• Entry DOI: 10.2210/pdb6qk7/pdb
• EMDB information: 4571
• Descriptor: Elongator complex protein 1, Elongator complex protein 2, Elongator complex protein 3, ... (5 entities in total)
• Functional Keywords: elongator, yeast, trna modification, elp123, translation
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 4
• Total formula weight: 460209.90

Authors

Dauden, M.I.,Jaciuk, M.,Glatt, S. (deposition date: 2019-01-28, release date: 2019-07-17, Last modification date: 2024-05-15)

Primary citation

Dauden, M.I.,Jaciuk, M.,Weis, F.,Lin, T.Y.,Kleindienst, C.,Abbassi, N.E.H.,Khatter, H.,Krutyholowa, R.,Breunig, K.D.,Kosinski, J.,Muller, C.W.,Glatt, S.
Molecular basis of tRNA recognition by the Elongator complex.
Sci Adv, 5:eaaw2326-eaaw2326, 2019

PubMed Abstract: The highly conserved Elongator complex modifies transfer RNAs (tRNAs) in their wobble base position, thereby regulating protein synthesis and ensuring proteome stability. The precise mechanisms of tRNA recognition and its modification reaction remain elusive. Here, we show cryo-electron microscopy structures of the catalytic subcomplex of Elongator and its tRNA-bound state at resolutions of 3.3 and 4.4 Å. The structures resolve details of the catalytic site, including the substrate tRNA, the iron-sulfur cluster, and a SAM molecule, which are all validated by mutational analyses in vitro and in vivo. tRNA binding induces conformational rearrangements, which precisely position the targeted anticodon base in the active site. Our results provide the molecular basis for substrate recognition of Elongator, essential to understand its cellular function and role in neurodegenerative diseases and cancer.

PubMed: 31309145
DOI: 10.1126/sciadv.aaw2326

Experimental method

ELECTRON MICROSCOPY (3.3 Å)