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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: 9g8o | ||||||||||||||||||
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| タイトル | human 40S ribosome bound by a SKI238-exosome complex | ||||||||||||||||||
要素 |
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キーワード | RIBOSOME / RNA-binding / RNA-degradation / cytoplasm / helicase | ||||||||||||||||||
| 機能・相同性 | 機能・相同性情報DNA deamination / nucleolar exosome (RNase complex) / exoribonuclease II / exoribonuclease II activity / Dom34-Hbs1 complex / nuclear-transcribed mRNA catabolic process, no-go decay / CUT catabolic process / U1 snRNA 3'-end processing / Ski complex / U5 snRNA 3'-end processing ...DNA deamination / nucleolar exosome (RNase complex) / exoribonuclease II / exoribonuclease II activity / Dom34-Hbs1 complex / nuclear-transcribed mRNA catabolic process, no-go decay / CUT catabolic process / U1 snRNA 3'-end processing / Ski complex / U5 snRNA 3'-end processing / TRAMP-dependent tRNA surveillance pathway / exosome (RNase complex) / cytoplasmic exosome (RNase complex) / mRNA decay by 3' to 5' exoribonuclease / U4 snRNA 3'-end processing / nuclear polyadenylation-dependent rRNA catabolic process / poly(A)-dependent snoRNA 3'-end processing / Cdc73/Paf1 complex / nuclear exosome (RNase complex) / nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay / nuclear-transcribed mRNA catabolic process, non-stop decay / exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA / negative regulation of myeloid cell differentiation / ATF4 activates genes in response to endoplasmic reticulum stress / Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA / 3'-5' RNA helicase activity / positive regulation of isotype switching / histone mRNA catabolic process / nuclear mRNA surveillance / rRNA catabolic process / Nuclear RNA decay / 7S RNA binding / mRNA 3'-UTR AU-rich region binding / isotype switching / negative regulation of endoplasmic reticulum unfolded protein response / ribosome disassembly / oxidized pyrimidine DNA binding / response to TNF agonist / positive regulation of base-excision repair / RNA catabolic process / positive regulation of ubiquitin-protein transferase activity / positive regulation of respiratory burst involved in inflammatory response / positive regulation of gastrulation / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / protein tyrosine kinase inhibitor activity / IRE1-RACK1-PP2A complex / positive regulation of Golgi to plasma membrane protein transport / nucleolus organization / positive regulation of DNA-templated transcription initiation / TNFR1-mediated ceramide production / negative regulation of RNA splicing / KSRP (KHSRP) binds and destabilizes mRNA / maturation of 5.8S rRNA / neural crest cell differentiation / supercoiled DNA binding / NF-kappaB complex / negative regulation of DNA repair / cytoplasmic translational initiation / oxidized purine DNA binding / cysteine-type endopeptidase activator activity involved in apoptotic process / negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide / rRNA modification in the nucleus and cytosol / negative regulation of bicellular tight junction assembly / ubiquitin-like protein conjugating enzyme binding / regulation of establishment of cell polarity / negative regulation of phagocytosis / erythrocyte homeostasis / cytoplasmic side of rough endoplasmic reticulum membrane / Formation of the ternary complex, and subsequently, the 43S complex / nuclear chromosome / ion channel inhibitor activity / laminin receptor activity / mRNA catabolic process / protein kinase A binding / pigmentation / Ribosomal scanning and start codon recognition / Association of TriC/CCT with target proteins during biosynthesis / positive regulation of mitochondrial depolarization / Translation initiation complex formation / negative regulation of Wnt signaling pathway / fibroblast growth factor binding / monocyte chemotaxis / BH3 domain binding / Protein hydroxylation / negative regulation of translational frameshifting / regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway / TOR signaling / positive regulation of GTPase activity / SARS-CoV-1 modulates host translation machinery / mTORC1-mediated signalling / iron-sulfur cluster binding / regulation of cell division / nuclear-transcribed mRNA catabolic process / Peptide chain elongation / cellular response to ethanol / Selenocysteine synthesis / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / Formation of a pool of free 40S subunits / negative regulation of protein binding 類似検索 - 分子機能 | ||||||||||||||||||
| 生物種 | Homo sapiens (ヒト) Cricket paralysis virus (ウイルス) | ||||||||||||||||||
| 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: 3.4 Å | ||||||||||||||||||
データ登録者 | Koegel, A. / Keidel, A. / Loukeri, M.J. / Kuhn, C.C. / Langer, L.M. / Schaefer, I.B. / Conti, E. | ||||||||||||||||||
| 資金援助 | ドイツ, European Union, デンマーク, 5件
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引用 | ジャーナル: Nature / 年: 2024タイトル: Structural basis of mRNA decay by the human exosome-ribosome supercomplex. 著者: Alexander Kögel / Achim Keidel / Matina-Jasemi Loukeri / Christopher C Kuhn / Lukas M Langer / Ingmar B Schäfer / Elena Conti / ![]() 要旨: The interplay between translation and mRNA decay is widespread in human cells. In quality-control pathways, exonucleolytic degradation of mRNA associated with translating ribosomes is mediated ...The interplay between translation and mRNA decay is widespread in human cells. In quality-control pathways, exonucleolytic degradation of mRNA associated with translating ribosomes is mediated largely by the cytoplasmic exosome, which includes the exoribonuclease complex EXO10 and the helicase complex SKI238 (refs. ). The helicase can extract mRNA from the ribosome and is expected to transfer it to the exoribonuclease core through a bridging factor, HBS1L3 (also known as SKI7), but the mechanisms of this molecular handover remain unclear. Here we reveal how human EXO10 is recruited by HBS1L3 (SKI7) to an active ribosome-bound SKI238 complex. We show that rather than a sequential handover, a direct physical coupling mechanism takes place, which culminates in the formation of a cytoplasmic exosome-ribosome supercomplex. Capturing the structure during active decay reveals a continuous path in which an RNA substrate threads from the 80S ribosome through the SKI2 helicase into the exoribonuclease active site of the cytoplasmic exosome complex. The SKI3 subunit of the complex directly binds to HBS1L3 (SKI7) and also engages a surface of the 40S subunit, establishing a recognition platform in collided disomes. Exosome and ribosome thus work together as a single structural and functional unit in co-translational mRNA decay, coordinating their activities in a transient supercomplex. | ||||||||||||||||||
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構造の表示
| 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 | 9g8o.cif.gz | 3.1 MB | 表示 | PDBx/mmCIF形式 |
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| PDB形式 | pdb9g8o.ent.gz | 表示 | PDB形式 | |
| PDBx/mmJSON形式 | 9g8o.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/g8/9g8o ftp://data.pdbj.org/pub/pdb/validation_reports/g8/9g8o | HTTPS FTP |
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-関連構造データ
| 関連構造データ | ![]() 51134MC ![]() 9g8mC ![]() 9g8nC ![]() 9g8pC ![]() 9g8qC ![]() 9g8rC 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 F&H 検索 |
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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 , 7種, 8分子 BCDAEMSfSg
| #1: タンパク質 | 分子量: 176064.750 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: SKIC3, KIAA0372, TTC37発現宿主: ![]() 参照: UniProt: Q6PGP7 | ||||||||||
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| #2: タンパク質 | 分子量: 33617.465 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: WDR61発現宿主: ![]() 参照: UniProt: Q9GZS3 #9: タンパク質 | | 分子量: 137913.688 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: SKIV2L, DDX13, SKI2W, SKIV2, W発現宿主: ![]() 参照: UniProt: Q15477, 加水分解酵素; 酸無水物に作用; 酸無水物に作用・細胞または細胞小器官の運動に関与 #10: タンパク質 | | 分子量: 30196.131 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: HBS1L, HBS1, KIAA1038 / 発現宿主: ![]() 参照: UniProt: Q9Y450, 加水分解酵素; 酸無水物に作用; GTPに作用・細胞または細胞小器官の運動に関与 #16: タンパク質 | | 分子量: 125229.984 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: DIS3L, DIS3L1, KIAA1955 / 発現宿主: ![]() #49: タンパク質 | | 分子量: 18004.041 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: P62979#50: タンパク質 | | 分子量: 35115.652 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: P63244 |
-Exosome complex component ... , 9種, 9分子 FJKLNOGHI
| #3: タンパク質 | 分子量: 32216.762 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: EXOSC7, KIAA0116, RRP42 / 発現宿主: ![]() |
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| #4: タンパク質 | 分子量: 21835.100 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: EXOSC1, CSL4, CGI-108 / 発現宿主: ![]() |
| #5: タンパク質 | 分子量: 49370.312 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: EXOSC9, PMSCL1 / 発現宿主: ![]() |
| #6: タンパク質 | 分子量: 30429.893 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: EXOSC8, OIP2, RRP43 / 発現宿主: ![]() |
| #7: タンパク質 | 分子量: 26416.996 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: EXOSC4, RRP41, SKI6 / 発現宿主: ![]() |
| #8: タンパク質 | 分子量: 25636.312 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: EXOSC5, CML28, RRP46 / 発現宿主: ![]() |
| #11: タンパク質 | 分子量: 28267.127 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: EXOSC6, MTR3 / 発現宿主: ![]() |
| #12: タンパク質 | 分子量: 29940.502 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: EXOSC3, RRP40, CGI-102 / 発現宿主: ![]() |
| #13: タンパク質 | 分子量: 33190.355 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: EXOSC2, RRP4 / 発現宿主: ![]() |
-RNA鎖 , 2種, 2分子 XS2
| #14: RNA鎖 | 分子量: 79333.953 Da / 分子数: 1 / 由来タイプ: 合成 / 由来: (合成) Cricket paralysis virus (ウイルス) |
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| #17: RNA鎖 | 分子量: 602752.875 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) |
-タンパク質・ペプチド , 1種, 1分子 Ln
| #15: タンパク質・ペプチド | 分子量: 3473.451 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: P62945 |
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+40S ribosomal protein ... , 31種, 31分子 SASBSCSDSESFSGSHSISJSKSLSMSNSOSPSQSRSSSTSUSVSWSXSYSZSaSbScSdSe
-詳細
| Has protein modification | N |
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-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 40S ribosome bound by a SKI238-exosome complex タイプ: RIBOSOME Entity ID: #14, #34-#39, #41, #44, #46, #15, #47, #49-#50, #20, #24, #17, #27, #30, #18, #31, #19, #32, #21, #40, #22, #42, #9, #1-#2, #23, #43, #3, #11-#13, #4-#5, #10, #16, #6-#8, #25, #45, #26, #48, #28-#29, #33 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) |
| 由来(組換発現) | 生物種: ![]() |
| 緩衝液 | pH: 7.4 |
| 試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
| 試料支持 | グリッドのサイズ: 200 divisions/in. / グリッドのタイプ: Quantifoil R2/1 |
| 急速凍結 | 凍結剤: ETHANE-PROPANE |
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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: FLOOD BEAM |
| 電子レンズ | モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 2400 nm / 最小 デフォーカス(公称値): 600 nm |
| 撮影 | 電子線照射量: 64.2 e/Å2 フィルム・検出器のモデル: GATAN K3 BIOQUANTUM (6k x 4k) |
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解析
| EMソフトウェア | 名称: PHENIX / バージョン: 1.20.1_4487: / カテゴリ: モデル精密化 | ||||||||||||||||||||||||
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| CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3次元再構成 | 解像度: 3.4 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 53460 / 対称性のタイプ: POINT | ||||||||||||||||||||||||
| 拘束条件 |
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ムービー
コントローラー
万見について




Homo sapiens (ヒト)
Cricket paralysis virus (ウイルス)
ドイツ, European Union,
デンマーク, 5件
引用











PDBj
































































FIELD EMISSION GUN