7MPI の概要
エントリーDOI | 10.2210/pdb7mpi/pdb |
EMDBエントリー | 23934 |
分子名称 | 40S ribosomal protein S0-A, 40S ribosomal protein S9-A, 40S ribosomal protein S10-A, ... (81 entities in total) |
機能のキーワード | yeast, 80s complex, chemical modification, ribosome |
由来する生物種 | Saccharomyces cerevisiae (Baker's yeast) 詳細 |
タンパク質・核酸の鎖数 | 79 |
化学式量合計 | 2940751.60 |
構造登録者 | |
主引用文献 | Zhao, Y.,Rai, J.,Yu, H.,Li, H. CryoEM structures of pseudouridine-free ribosome suggest impacts of chemical modifications on ribosome conformations. Structure, 30:983-, 2022 Cited by PubMed Abstract: Pseudouridine, the most abundant form of RNA modification, is known to play important roles in ribosome function. Mutations in human DKC1, the pseudouridine synthase responsible for catalyzing the ribosome RNA modification, cause translation deficiencies and are associated with a complex cancer predisposition. The structural basis for how pseudouridine impacts ribosome function remains uncharacterized. Here, we characterized structures and conformations of a fully modified and a pseudouridine-free ribosome from Saccharomyces cerevisiae in the absence of ligands or when bound with translocation inhibitor cycloheximide by electron cryomicroscopy. In the modified ribosome, the rearranged N1 atom of pseudouridine is observed to stabilize key functional motifs by establishing predominately water-mediated close contacts with the phosphate backbone. The pseudouridine-free ribosome, however, is devoid of such interactions and displays conformations reflective of abnormal inter-subunit movements. The erroneous motions of the pseudouridine-free ribosome may explain its observed deficiencies in translation. PubMed: 35489333DOI: 10.1016/j.str.2022.04.002 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.05 Å) |
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