8E3S

CryoEM structure of yeast Arginyltransferase 1 (ATE1)

Summary for 8E3S

• Entry DOI: 10.2210/pdb8e3s/pdb
• EMDB information: 27871
• Descriptor: Arginyl-tRNA--protein transferase 1, ZINC ION (2 entities in total)
• Functional Keywords: arginyltransferase, post-translational modification, enzyme, transferase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 58066.69

Authors

Huang, W.,Zhang, Y.,Taylor, D.J. (deposition date: 2022-08-17, release date: 2023-04-26, Last modification date: 2024-05-01)

Primary citation

Abeywansha, T.,Huang, W.,Ye, X.,Nawrocki, A.,Lan, X.,Jankowsky, E.,Taylor, D.J.,Zhang, Y.
The structural basis of tRNA recognition by arginyl-tRNA-protein transferase.
Nat Commun, 14:2232-2232, 2023

PubMed Abstract: Arginyl-tRNA-protein transferase 1 (ATE1) is a master regulator of protein homeostasis, stress response, cytoskeleton maintenance, and cell migration. The diverse functions of ATE1 arise from its unique enzymatic activity to covalently attach an arginine onto its protein substrates in a tRNA-dependent manner. However, how ATE1 (and other aminoacyl-tRNA transferases) hijacks tRNA from the highly efficient ribosomal protein synthesis pathways and catalyzes the arginylation reaction remains a mystery. Here, we describe the three-dimensional structures of Saccharomyces cerevisiae ATE1 with and without its tRNA cofactor. Importantly, the putative substrate binding domain of ATE1 adopts a previously uncharacterized fold that contains an atypical zinc-binding site critical for ATE1 stability and function. The unique recognition of tRNA by ATE1 is coordinated through interactions with the major groove of the acceptor arm of tRNA. Binding of tRNA induces conformational changes in ATE1 that helps explain the mechanism of substrate arginylation.

PubMed: 37076488
DOI: 10.1038/s41467-023-38004-8

Experimental method

ELECTRON MICROSCOPY (3.1 Å)