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-Structure paper
Title | The structural basis of tRNA recognition by arginyl-tRNA-protein transferase. |
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Journal, issue, pages | Nat Commun, Vol. 14, Issue 1, Page 2232, Year 2023 |
Publish date | Apr 19, 2023 |
Authors | Thilini Abeywansha / Wei Huang / Xuan Ye / Allison Nawrocki / Xin Lan / Eckhard Jankowsky / Derek J Taylor / Yi Zhang / |
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 ...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. |
External links | Nat Commun / PubMed:37076488 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.1 - 3.6 Å |
Structure data | EMDB-27871, PDB-8e3s: EMDB-29638, PDB-8fzr: |
Chemicals | ChemComp-ZN: |
Source |
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Keywords | TRANSFERASE / Arginyltransferase / post-translational modification / enzyme / TRANSFERASE/RNA / TRANSFERASE-RNA complex |