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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: 6ff7 | ||||||
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| タイトル | human Bact spliceosome core structure | ||||||
要素 |
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キーワード | SPLICING / spliceosome / human / HELA / BACT / dynamics | ||||||
| 機能・相同性 | 機能・相同性情報post-spliceosomal complex / RES complex / negative regulation of chemokine-mediated signaling pathway / snoRNA splicing / U11/U12 snRNP / regulation of retinoic acid receptor signaling pathway / post-mRNA release spliceosomal complex / 3'-5' RNA helicase activity / U2 snRNP binding / U7 snRNA binding ...post-spliceosomal complex / RES complex / negative regulation of chemokine-mediated signaling pathway / snoRNA splicing / U11/U12 snRNP / regulation of retinoic acid receptor signaling pathway / post-mRNA release spliceosomal complex / 3'-5' RNA helicase activity / U2 snRNP binding / U7 snRNA binding / histone pre-mRNA DCP binding / generation of catalytic spliceosome for first transesterification step / U7 snRNP / cis assembly of pre-catalytic spliceosome / histone pre-mRNA 3'end processing complex / regulation of vitamin D receptor signaling pathway / SLBP independent Processing of Histone Pre-mRNAs / SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs / spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) / B-WICH complex / miRNA processing / nuclear retinoic acid receptor binding / embryonic brain development / oocyte development / protein methylation / alternative mRNA splicing, via spliceosome / U12-type spliceosomal complex / poly(A) binding / 7-methylguanosine cap hypermethylation / U1 snRNP binding / U2-type catalytic step 1 spliceosome / C2H2 zinc finger domain binding / RNA splicing, via transesterification reactions / methylosome / pICln-Sm protein complex / pre-mRNA binding / regulation of mRNA splicing, via spliceosome / positive regulation of mRNA splicing, via spliceosome / snRNP binding / mRNA 3'-end processing / blastocyst formation / sno(s)RNA-containing ribonucleoprotein complex / small nuclear ribonucleoprotein complex / splicing factor binding / Notch binding / host-mediated activation of viral transcription / SMN-Sm protein complex / spliceosomal tri-snRNP complex / mRNA cis splicing, via spliceosome / U2-type precatalytic spliceosome / P granule / positive regulation of vitamin D receptor signaling pathway / commitment complex / telomerase holoenzyme complex / nuclear vitamin D receptor binding / U2-type prespliceosome assembly / telomerase RNA binding / U2-type spliceosomal complex / Transport of Mature mRNA derived from an Intron-Containing Transcript / Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells / RUNX3 regulates NOTCH signaling / U2-type catalytic step 2 spliceosome / NOTCH4 Intracellular Domain Regulates Transcription / SAGA complex / U2 snRNP / RHOBTB1 GTPase cycle / U1 snRNP / RNA Polymerase II Transcription Termination / U4 snRNP / NOTCH3 Intracellular Domain Regulates Transcription / positive regulation of neurogenesis / U2-type prespliceosome / positive regulation of transcription by RNA polymerase III / inner cell mass cell proliferation / protein peptidyl-prolyl isomerization / K63-linked polyubiquitin modification-dependent protein binding / ubiquitin-ubiquitin ligase activity / nuclear androgen receptor binding / cyclosporin A binding / precatalytic spliceosome / generation of catalytic spliceosome for second transesterification step / WD40-repeat domain binding / Notch-HLH transcription pathway / lipid biosynthetic process / Formation of paraxial mesoderm / pattern recognition receptor activity / SMAD binding / positive regulation of transforming growth factor beta receptor signaling pathway / regulation of RNA splicing / spliceosomal complex assembly / mRNA 3'-splice site recognition / positive regulation of transcription by RNA polymerase I / mRNA Splicing - Minor Pathway / spliceosomal tri-snRNP complex assembly / Prp19 complex / U5 snRNA binding / U5 snRNP / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / protein K63-linked ubiquitination / blastocyst development 類似検索 - 分子機能 | ||||||
| 生物種 | Homo sapiens (ヒト) | ||||||
| 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: 4.5 Å | ||||||
データ登録者 | Haselbach, D. / Komarov, I. / Agafonov, D. / Hartmuth, K. / Graf, B. / Kastner, B. / Luehrmann, R. / Stark, H. | ||||||
引用 | ジャーナル: Cell / 年: 2018タイトル: Structure and Conformational Dynamics of the Human Spliceosomal B Complex. 著者: David Haselbach / Ilya Komarov / Dmitry E Agafonov / Klaus Hartmuth / Benjamin Graf / Olexandr Dybkov / Henning Urlaub / Berthold Kastner / Reinhard Lührmann / Holger Stark / ![]() 要旨: The spliceosome is a highly dynamic macromolecular complex that precisely excises introns from pre-mRNA. Here we report the cryo-EM 3D structure of the human B spliceosome at 3.4 Å resolution. In ...The spliceosome is a highly dynamic macromolecular complex that precisely excises introns from pre-mRNA. Here we report the cryo-EM 3D structure of the human B spliceosome at 3.4 Å resolution. In the B state, the spliceosome is activated but not catalytically primed, so that it is functionally blocked prior to the first catalytic step of splicing. The spliceosomal core is similar to the yeast B spliceosome; important differences include the presence of the RNA helicase aquarius and peptidyl prolyl isomerases. To examine the overall dynamic behavior of the purified spliceosome, we developed a principal component analysis-based approach. Calculating the energy landscape revealed eight major conformational states, which we refined to higher resolution. Conformational differences of the highly flexible structural components between these eight states reveal how spliceosomal components contribute to the assembly of the spliceosome, allowing it to generate a dynamic interaction network required for its subsequent catalytic activation. | ||||||
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構造の表示
| ムービー |
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| 構造ビューア | 分子: Molmil Jmol/JSmol |
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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 | 6ff7.cif.gz | 2.8 MB | 表示 | PDBx/mmCIF形式 |
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| PDB形式 | pdb6ff7.ent.gz | 1.8 MB | 表示 | PDB形式 |
| PDBx/mmJSON形式 | 6ff7.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
| その他 | その他のダウンロード |
-検証レポート
| アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/ff/6ff7 ftp://data.pdbj.org/pub/pdb/validation_reports/ff/6ff7 | HTTPS FTP |
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-関連構造データ
| 関連構造データ | ![]() 4240MC ![]() 4233C ![]() 4234C ![]() 4235C ![]() 4236C ![]() 4237C ![]() 4238C ![]() 4239C ![]() 4247C ![]() 4248C ![]() 4249C ![]() 4250C ![]() 4251C ![]() 4252C ![]() 4253C ![]() 4254C ![]() 4255C ![]() 6ff4C 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 | |
| 電子顕微鏡画像生データ | EMPIAR-10160 (タイトル: Conformational Dynamics of human Bact spliceosomeData size: 2.8 TB Data #1: aligned and summed micrograph stack of human Bact spliceosome [micrographs - single frame] Data #2: aligned, dose-weighted and summed micrograph stack of human Bact spliceosome [micrographs - single frame]) |
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リンク
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集合体
| 登録構造単位 | ![]()
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| 1 |
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要素
+タンパク質 , 17種, 18分子 13ABCDLOQRVty0Ufmq
+RNA鎖 , 4種, 4分子 256Z
+Splicing factor 3A subunit ... , 3種, 3分子 79p
+Splicing factor 3B subunit ... , 5種, 6分子 8uvxzN
+Pre-mRNA-processing factor ... , 2種, 5分子 EGHIJ
+Pre-mRNA-splicing factor ... , 5種, 5分子 PKMTw
+Serine/arginine repetitive matrix protein ... , 2種, 2分子 SY
+Peptidyl-prolyl cis-trans isomerase ... , 2種, 2分子 so
+U5 small nuclear ribonucleoprotein ... , 2種, 2分子 Fr
+U2 small nuclear ribonucleoprotein ... , 2種, 2分子 WX
+Small nuclear ribonucleoprotein ... , 6種, 12分子 ahbicjdkelgn
+非ポリマー , 5種, 20分子 








-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: human Bact spliceosome / タイプ: COMPLEX / Entity ID: #1-#50 / 由来: NATURAL |
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| 分子量 | 実験値: NO |
| 由来(天然) | 生物種: Homo sapiens (ヒト) |
| 緩衝液 | pH: 7.6 |
| 試料 | 包埋: YES / シャドウイング: NO / 染色: NO / 凍結: YES |
| 試料支持 | グリッドの材料: COPPER / グリッドのサイズ: 200 divisions/in. / グリッドのタイプ: Quantifoil R3.5/1 |
| EM embedding | Material: ice |
| 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: FIELD EMISSION GUN / 加速電圧: 300 kV / 照射モード: SPOT SCAN |
| 電子レンズ | モード: BRIGHT FIELD |
| 撮影 | 電子線照射量: 40 e/Å2 / 検出モード: INTEGRATING フィルム・検出器のモデル: FEI FALCON III (4k x 4k) |
| 画像スキャン | サンプリングサイズ: 14 µm / 横: 4096 / 縦: 4096 |
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解析
| EMソフトウェア |
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| CTF補正 | タイプ: PHASE FLIPPING ONLY | ||||||||||||||||
| 対称性 | 点対称性: C1 (非対称) | ||||||||||||||||
| 3次元再構成 | 解像度: 4.5 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 165853 / 対称性のタイプ: POINT |
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万見について




Homo sapiens (ヒト)
引用
UCSF Chimera





















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