5GM6
Cryo-EM structure of the activated spliceosome (Bact complex) at 3.5 angstrom resolution
これはPDB形式変換不可エントリーです。
5GM6 の概要
| エントリーDOI | 10.2210/pdb5gm6/pdb |
| 関連するPDBエントリー | 5GMK |
| EMDBエントリー | 9524 9525 9526 9527 |
| 分子名称 | Pre-mRNA-splicing factor 8, RDS3 complex subunit 10, U2 snRNA, ... (47 entities in total) |
| 機能のキーワード | spliceosome, rna splicing, bact, catalytically activated, rna binding protein-rna complex, rna binding protein/rna |
| 由来する生物種 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 詳細 |
| タンパク質・核酸の鎖数 | 46 |
| 化学式量合計 | 2679389.46 |
| 構造登録者 | |
| 主引用文献 | Yan, C.,Wan, R.,Bai, R.,Huang, G.,Shi, Y. Structure of a yeast activated spliceosome at 3.5 angstrom resolution Science, 353:904-911, 2016 Cited by PubMed Abstract: Pre-messenger RNA (pre-mRNA) splicing is carried out by the spliceosome, which undergoes an intricate assembly and activation process. Here, we report an atomic structure of an activated spliceosome (known as the B(act) complex) from Saccharomyces cerevisiae, determined by cryo-electron microscopy at an average resolution of 3.52 angstroms. The final refined model contains U2 and U5 small nuclear ribonucleoprotein particles (snRNPs), U6 small nuclear RNA (snRNA), nineteen complex (NTC), NTC-related (NTR) protein, and a 71-nucleotide pre-mRNA molecule, which amount to 13,505 amino acids from 38 proteins and a combined molecular mass of about 1.6 megadaltons. The 5' exon is anchored by loop I of U5 snRNA, whereas the 5' splice site (5'SS) and the branch-point sequence (BPS) of the intron are specifically recognized by U6 and U2 snRNA, respectively. Except for coordination of the catalytic metal ions, the RNA elements at the catalytic cavity of Prp8 are mostly primed for catalysis. The catalytic latency is maintained by the SF3b complex, which encircles the BPS, and the splicing factors Cwc24 and Prp11, which shield the 5' exon-5'SS junction. This structure, together with those determined earlier, outlines a molecular framework for the pre-mRNA splicing reaction. PubMed: 27445306DOI: 10.1126/science.aag0291 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.5 Å) |
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