9YPG
GTPBP1*GCP*Phe-tRNA*ribosome in the GTPase activation-like state, Structure III
これはPDB形式変換不可エントリーです。
9YPG の概要
| エントリーDOI | 10.2210/pdb9ypg/pdb |
| EMDBエントリー | 73297 |
| 分子名称 | 28S ribosomal RNA, 60S ribosomal protein L7a, 60S ribosomal protein L9, ... (92 entities in total) |
| 機能のキーワード | gtpbp1, trna, gcp, complex, ribosome |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| タンパク質・核酸の鎖数 | 84 |
| 化学式量合計 | 3539579.15 |
| 構造登録者 | |
| 主引用文献 | Susorov, D.,Miscicka, A.,Golovenko, D.,Loveland, A.B.,Zinoviev, A.,Pestova, T.V.,Korostelev, A.A. Structural mechanism of mRNA decoding by mammalian GTPase GTPBP1. Nat Commun, 2025 Cited by PubMed Abstract: GTP-binding protein 1 (GTPBP1) is a widespread translational GTPase closely related to elongation factor eEF1A. The loss of GTPBP1 leads to neurodevelopmental and neurodegenerative disorders in animals. Although linked to translation and quality control mechanisms, GTPBP1 molecular functions remain largely obscure. Similarly to eEF1A, GTPBP1 delivers aminoacyl-tRNA to the ribosome, but the ensuing GTPBP1-mediated elongation is slow. Here, using cryo-EM of mammalian 80S ribosomal complexes bound to GTPBP1 and aa-tRNA with GTP or the non-hydrolysable analog GDPCP, we show that the distinct GTPBP1 architecture and interactions with tRNA underlie slow GTPBP1 dissociation after GTP hydrolysis, resulting in delayed tRNA accommodation. Slow dissociation correlates with an extended proofreading stage and higher accuracy of GTPBP1-mediated decoding, potentially allowing GTPBP1 to elicit its putative quality control functions. GTPBP1 visualization provides the foundation for mapping and elucidating GTPBP1 mutations associated with human diseases. PubMed: 41350250DOI: 10.1038/s41467-025-66833-2 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3 Å) |
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