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データを開く
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基本情報
登録情報 | データベース: PDB / ID: 8i0s | |||||||||||||||||||||||||||||||||||||||||||||
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タイトル | The cryo-EM structure of human Bact-II complex | |||||||||||||||||||||||||||||||||||||||||||||
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![]() | SPLICING / spliceosome / Bact-II complex / RNA splicing / PRP2 / branching | |||||||||||||||||||||||||||||||||||||||||||||
機能・相同性 | ![]() negative regulation of chemokine-mediated signaling pathway / snoRNA splicing / U11/U12 snRNP / regulation of retinoic acid receptor signaling pathway / post-mRNA release spliceosomal complex / U2 snRNP binding / U7 snRNA binding / histone pre-mRNA DCP binding / 3'-5' RNA helicase activity / U7 snRNP ...negative regulation of chemokine-mediated signaling pathway / snoRNA splicing / U11/U12 snRNP / regulation of retinoic acid receptor signaling pathway / post-mRNA release spliceosomal complex / U2 snRNP binding / U7 snRNA binding / histone pre-mRNA DCP binding / 3'-5' RNA helicase activity / U7 snRNP / generation of catalytic spliceosome for first transesterification step / histone pre-mRNA 3'end processing complex / cis assembly of pre-catalytic spliceosome / regulation of vitamin D receptor signaling pathway / SLBP independent Processing of Histone Pre-mRNAs / SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs / B-WICH complex / spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) / nuclear retinoic acid receptor binding / embryonic brain development / protein methylation / U12-type spliceosomal complex / poly(A) binding / 7-methylguanosine cap hypermethylation / RNA splicing, via transesterification reactions / U1 snRNP binding / sno(s)RNA-containing ribonucleoprotein complex / methylosome / regulation of mRNA splicing, via spliceosome / pICln-Sm protein complex / C2H2 zinc finger domain binding / U2-type catalytic step 1 spliceosome / pre-mRNA binding / positive regulation of mRNA splicing, via spliceosome / snRNP binding / small nuclear ribonucleoprotein complex / splicing factor binding / SMN-Sm protein complex / P granule / host-mediated activation of viral transcription / spliceosomal tri-snRNP complex / U2-type precatalytic spliceosome / telomerase RNA binding / U2-type spliceosomal complex / positive regulation of vitamin D receptor signaling pathway / telomerase holoenzyme complex / commitment complex / mRNA cis splicing, via spliceosome / U2-type prespliceosome assembly / nuclear vitamin D receptor binding / Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells / Notch binding / RUNX3 regulates NOTCH signaling / U2-type catalytic step 2 spliceosome / positive regulation of neurogenesis / NOTCH4 Intracellular Domain Regulates Transcription / SAGA complex / U4 snRNP / U2 snRNP / RNA Polymerase II Transcription Termination / U1 snRNP / NOTCH3 Intracellular Domain Regulates Transcription / protein peptidyl-prolyl isomerization / Basigin interactions / U2-type prespliceosome / positive regulation of transcription by RNA polymerase III / WD40-repeat domain binding / ubiquitin-ubiquitin ligase activity / nuclear androgen receptor binding / K63-linked polyubiquitin modification-dependent protein binding / precatalytic spliceosome / cyclosporin A binding / pattern recognition receptor activity / Notch-HLH transcription pathway / Formation of paraxial mesoderm / positive regulation of transforming growth factor beta receptor signaling pathway / SMAD binding / spliceosomal complex assembly / positive regulation of transcription by RNA polymerase I / regulation of RNA splicing / mRNA Splicing - Minor Pathway / mRNA 3'-splice site recognition / spliceosomal tri-snRNP complex assembly / blastocyst development / Prp19 complex / RNA polymerase II CTD heptapeptide repeat P3 isomerase activity / RNA polymerase II CTD heptapeptide repeat P6 isomerase activity / U5 snRNA binding / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / protein localization to nucleus / U5 snRNP / positive regulation of G1/S transition of mitotic cell cycle / U2 snRNA binding / U6 snRNA binding / pre-mRNA intronic binding / spliceosomal snRNP assembly / positive regulation of viral genome replication / RNA processing / Cajal body / regulation of DNA repair 類似検索 - 分子機能 | |||||||||||||||||||||||||||||||||||||||||||||
生物種 | ![]() ![]() | |||||||||||||||||||||||||||||||||||||||||||||
手法 | 電子顕微鏡法 / 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 4.2 Å | |||||||||||||||||||||||||||||||||||||||||||||
![]() | Zhan, X. / Lu, Y. / Shi, Y. | |||||||||||||||||||||||||||||||||||||||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Molecular basis for the activation of human spliceosome. 著者: Xiechao Zhan / Yichen Lu / Yigong Shi / ![]() 要旨: The spliceosome executes pre-mRNA splicing through four sequential stages: assembly, activation, catalysis, and disassembly. Activation of the spliceosome, namely remodeling of the pre-catalytic ...The spliceosome executes pre-mRNA splicing through four sequential stages: assembly, activation, catalysis, and disassembly. Activation of the spliceosome, namely remodeling of the pre-catalytic spliceosome (B complex) into the activated spliceosome (B complex) and the catalytically activated spliceosome (B complex), involves major flux of protein components and structural rearrangements. Relying on a splicing inhibitor, we have captured six intermediate states between the B and B complexes: pre-B, B-I, B-II, B-III, B-IV, and post-B. Their cryo-EM structures, together with an improved structure of the catalytic step I spliceosome (C complex), reveal how the catalytic center matures around the internal stem loop of U6 snRNA, how the branch site approaches 5'-splice site, how the RNA helicase PRP2 rearranges to bind pre-mRNA, and how U2 snRNP undergoes remarkable movement to facilitate activation. We identify a previously unrecognized key role of PRP2 in spliceosome activation. Our study recapitulates a molecular choreography of the human spliceosome during its catalytic activation. | |||||||||||||||||||||||||||||||||||||||||||||
履歴 |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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ダウンロードとリンク
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ダウンロード
PDBx/mmCIF形式 | ![]() | 2.9 MB | 表示 | ![]() |
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PDB形式 | ![]() | 表示 | ![]() | |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
文書・要旨 | ![]() | 2.3 MB | 表示 | ![]() |
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文書・詳細版 | ![]() | 2.9 MB | 表示 | |
XML形式データ | ![]() | 431.9 KB | 表示 | |
CIF形式データ | ![]() | 684.7 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
関連構造データ | ![]() 35108MC ![]() 8i0pC ![]() 8i0rC ![]() 8i0tC ![]() 8i0uC ![]() 8i0vC ![]() 8i0wC M: このデータのモデリングに利用したマップデータ C: 同じ文献を引用 ( |
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類似構造データ | 類似検索 - 機能・相同性 ![]() |
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リンク
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集合体
登録構造単位 | ![]()
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要素
+タンパク質 , 15種, 16分子 ACJKLNPQRTU7y9am
+RNA鎖 , 4種, 4分子 BFGH
+U5 small nuclear ribonucleoprotein ... , 2種, 2分子 DE
+Pre-mRNA-splicing factor ... , 4種, 4分子 IOVX
+Peptidyl-prolyl cis-trans isomerase-like ... , 2種, 2分子 SY
+Splicing factor 3B subunit ... , 5種, 5分子 13245
+U2 small nuclear ribonucleoprotein ... , 2種, 2分子 po
+Splicing factor 3A subunit ... , 3種, 3分子 wvu
+Small nuclear ribonucleoprotein ... , 6種, 12分子 bnchdiejfkgl
+非ポリマー , 4種, 16分子 






+詳細
-実験情報
-実験
実験 | 手法: 電子顕微鏡法 |
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EM実験 | 試料の集合状態: PARTICLE / 3次元再構成法: 単粒子再構成法 |
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試料調製
構成要素 | 名称: The human Bact-II complex / タイプ: COMPLEX Entity ID: #1-#3, #5, #21, #11, #6, #8, #24-#25, #10, #12, #15, #26-#27, #16, #9, #28-#31, #17, #19, #32-#33, #7, #14, #13, #20, #34, #4, #22-#23, #18, #35-#43 由来: NATURAL |
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由来(天然) | 生物種: ![]() |
緩衝液 | pH: 7.9 |
試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
急速凍結 | 凍結剤: ETHANE |
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電子顕微鏡撮影
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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顕微鏡 | モデル: FEI TITAN KRIOS |
電子銃 | 電子線源: ![]() |
電子レンズ | モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 2000 nm / 最小 デフォーカス(公称値): 1400 nm |
撮影 | 電子線照射量: 50 e/Å2 / 検出モード: SUPER-RESOLUTION / フィルム・検出器のモデル: GATAN K3 (6k x 4k) |
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解析
ソフトウェア | 名称: PHENIX / バージョン: 1.17.1_3660: / 分類: 精密化 | ||||||||||||||||||||||||
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EMソフトウェア | 名称: PHENIX / カテゴリ: モデル精密化 | ||||||||||||||||||||||||
CTF補正 | タイプ: NONE | ||||||||||||||||||||||||
3次元再構成 | 解像度: 4.2 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 13372 / 対称性のタイプ: POINT | ||||||||||||||||||||||||
拘束条件 |
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