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CryoEM structure of yeast Arginyltransferase 1 (ATE1)
Structural highlights
FunctionATE1_YEAST Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway (PubMed:2185248). Does not arginylate cysteine residues (By similarity).[1] Publication Abstract from PubMedArginyl-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(Arg) 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. The structural basis of tRNA recognition by arginyl-tRNA-protein transferase.,Abeywansha T, Huang W, Ye X, Nawrocki A, Lan X, Jankowsky E, Taylor DJ, Zhang Y Nat Commun. 2023 Apr 19;14(1):2232. doi: 10.1038/s41467-023-38004-8. PMID:37076488[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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