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-Structure paper
タイトル | The structural basis of tRNA recognition by arginyl-tRNA-protein transferase. |
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ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 2232, Year 2023 |
掲載日 | 2023年4月19日 |
![]() | Thilini Abeywansha / Wei Huang / Xuan Ye / Allison Nawrocki / Xin Lan / Eckhard Jankowsky / Derek J Taylor / Yi Zhang / ![]() |
PubMed 要旨 | 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. |
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手法 | EM (単粒子) |
解像度 | 3.1 - 3.6 Å |
構造データ | EMDB-27871, PDB-8e3s: EMDB-29638, PDB-8fzr: |
化合物 | ![]() ChemComp-ZN: |
由来 |
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![]() | TRANSFERASE / Arginyltransferase / post-translational modification / enzyme / TRANSFERASE/RNA / TRANSFERASE-RNA complex |