+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 7qgg | ||||||||||||
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タイトル | Neuronal RNA granules are ribosome complexes stalled at the pre-translocation state | ||||||||||||
要素 |
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キーワード | RIBOSOME / RNA granule / rat | ||||||||||||
機能・相同性 | 機能・相同性情報 regulation of myeloid dendritic cell activation / positive regulation of selenocysteine incorporation / Protein hydroxylation / mTORC1-mediated signalling / Translesion synthesis by REV1 / Recognition of DNA damage by PCNA-containing replication complex / APC/C:Cdc20 mediated degradation of Cyclin B / APC-Cdc20 mediated degradation of Nek2A / Activated NOTCH1 Transmits Signal to the Nucleus / Downregulation of TGF-beta receptor signaling ...regulation of myeloid dendritic cell activation / positive regulation of selenocysteine incorporation / Protein hydroxylation / mTORC1-mediated signalling / Translesion synthesis by REV1 / Recognition of DNA damage by PCNA-containing replication complex / APC/C:Cdc20 mediated degradation of Cyclin B / APC-Cdc20 mediated degradation of Nek2A / Activated NOTCH1 Transmits Signal to the Nucleus / Downregulation of TGF-beta receptor signaling / Regulation of FZD by ubiquitination / Regulation of TNFR1 signaling / TNFR1-induced NF-kappa-B signaling pathway / Translesion synthesis by POLK / Translesion synthesis by POLI / Termination of translesion DNA synthesis / Gap-filling DNA repair synthesis and ligation in GG-NER / Formation of TC-NER Pre-Incision Complex / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / Fanconi Anemia Pathway / Regulation of TP53 Degradation / Regulation of TP53 Activity through Methylation / Cyclin D associated events in G1 / Stabilization of p53 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / ER Quality Control Compartment (ERQC) / Interferon alpha/beta signaling / Endosomal Sorting Complex Required For Transport (ESCRT) / Negative regulators of DDX58/IFIH1 signaling / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / IKK complex recruitment mediated by RIP1 / IRAK2 mediated activation of TAK1 complex / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Alpha-protein kinase 1 signaling pathway / Inactivation of CSF3 (G-CSF) signaling / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / Regulation of NF-kappa B signaling / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / NOD1/2 Signaling Pathway / activated TAK1 mediates p38 MAPK activation / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / DNA Damage Recognition in GG-NER / Formation of Incision Complex in GG-NER / Dual Incision in GG-NER / E3 ubiquitin ligases ubiquitinate target proteins / Translesion Synthesis by POLH / Downregulation of ERBB2:ERBB3 signaling / TCF dependent signaling in response to WNT / Regulation of innate immune responses to cytosolic DNA / HDR through Homologous Recombination (HRR) / Downregulation of ERBB2 signaling / Regulation of signaling by CBL / Ovarian tumor domain proteases / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / NOTCH3 Activation and Transmission of Signal to the Nucleus / Interleukin-1 signaling / cellular response to Thyroid stimulating hormone / Downregulation of ERBB4 signaling / Deactivation of the beta-catenin transactivating complex / Negative regulation of MET activity / Translation initiation complex formation / Formation of the ternary complex, and subsequently, the 43S complex / Ribosomal scanning and start codon recognition / Protein methylation / Regulation of PTEN localization / L13a-mediated translational silencing of Ceruloplasmin expression / SRP-dependent cotranslational protein targeting to membrane / Josephin domain DUBs / Formation of a pool of free 40S subunits / GTP hydrolysis and joining of the 60S ribosomal subunit / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / RMTs methylate histone arginines / Major pathway of rRNA processing in the nucleolus and cytosol / Pexophagy / Stimuli-sensing channels / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / 5.8S rRNA binding / Metalloprotease DUBs / Regulation of necroptotic cell death / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Autodegradation of Cdh1 by Cdh1:APC/C / SCF-beta-TrCP mediated degradation of Emi1 / APC/C:Cdc20 mediated degradation of Securin / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / SCF(Skp2)-mediated degradation of p27/p21 / NRIF signals cell death from the nucleus / NF-kB is activated and signals survival / Autodegradation of the E3 ubiquitin ligase COP1 / Asymmetric localization of PCP proteins / Degradation of DVL / Hedgehog ligand biogenesis / Dectin-1 mediated noncanonical NF-kB signaling / Degradation of GLI1 by the proteasome / Hedgehog 'on' state / TNFR2 non-canonical NF-kB pathway / NIK-->noncanonical NF-kB signaling 類似検索 - 分子機能 | ||||||||||||
生物種 | Rattus norvegicus (ドブネズミ) | ||||||||||||
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: 2.86 Å | ||||||||||||
データ登録者 | Pulk, A. / Kipper, K. / Mansour, A. | ||||||||||||
資金援助 | Estonia, 3件
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引用 | ジャーナル: J Mol Biol / 年: 2022 タイトル: Neuronal RNA granules are ribosome complexes stalled at the pre-translocation state. 著者: Kalle Kipper / Abbas Mansour / Arto Pulk / 要旨: The polarized cell morphology of neurons dictates many neuronal processes, including the axodendridic transport of specific mRNAs and subsequent translation. mRNAs together with ribosomes and RNA- ...The polarized cell morphology of neurons dictates many neuronal processes, including the axodendridic transport of specific mRNAs and subsequent translation. mRNAs together with ribosomes and RNA-binding proteins form RNA granules that are targeted to axodendrites for localized translation in neurons. It has been established that localized protein synthesis in neurons is essential for long-term memory formation, synaptic plasticity, and neurodegeneration. We have used proteomics and electron microscopy to characterize neuronal RNA granules (nRNAg) isolated from rat brain tissues or human neuroblastoma. We show that ribosome-containing RNA granules are morula-like structures when visualized by electron microscopy. Crosslinking-coupled mass-spectrometry identified a potential G3BP2 binding site on the ribosome near the eIF3d-binding site on the 40S ribosomal subunit. We used cryo-EM to resolve the structure of the ribosome-component of nRNAg. The cryo-EM reveals that predominant particles in nRNAg are 80S ribosomes, resembling the pre-translocation state where tRNA's are in the hybrid A/P and P/E site. We also describe a new kind of principal motion of the ribosome, which we call the rocking motion. | ||||||||||||
履歴 |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 7qgg.cif.gz | 5.4 MB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb7qgg.ent.gz | 表示 | PDB形式 | |
PDBx/mmJSON形式 | 7qgg.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
文書・要旨 | 7qgg_validation.pdf.gz | 1.6 MB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 7qgg_full_validation.pdf.gz | 1.7 MB | 表示 | |
XML形式データ | 7qgg_validation.xml.gz | 344.1 KB | 表示 | |
CIF形式データ | 7qgg_validation.cif.gz | 594.4 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/qg/7qgg ftp://data.pdbj.org/pub/pdb/validation_reports/qg/7qgg | HTTPS FTP |
-関連構造データ
関連構造データ | 13954MC 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 (文献) |
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類似構造データ | 類似検索 - 機能・相同性F&H 検索 |
-リンク
-集合体
登録構造単位 |
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1 |
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-要素
-RNA鎖 , 7種, 7分子 S2DEtuvw
#1: RNA鎖 | 分子量: 604241.188 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Rattus norvegicus (ドブネズミ) |
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#38: RNA鎖 | 分子量: 50449.812 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Rattus norvegicus (ドブネズミ) / 参照: GenBank: 57148 |
#39: RNA鎖 | 分子量: 38998.078 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Rattus norvegicus (ドブネズミ) / 参照: GenBank: 793860 |
#79: RNA鎖 | 分子量: 1553954.250 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Rattus norvegicus (ドブネズミ) |
#80: RNA鎖 | 分子量: 24414.451 Da / 分子数: 1 / 由来タイプ: 天然 詳細: A/P and P/E tRNAs. For some reason it has united the two tRNAs into one molecule, although these are different molecules with different sequences. As the structure contains heterogeneous ...詳細: A/P and P/E tRNAs. For some reason it has united the two tRNAs into one molecule, although these are different molecules with different sequences. As the structure contains heterogeneous population of tRNAs then the identity of tRNA is unknown. 由来: (天然) Rattus norvegicus (ドブネズミ) / 参照: GenBank: 1851728667 |
#81: RNA鎖 | 分子量: 24436.508 Da / 分子数: 1 / 由来タイプ: 天然 詳細: A/P and P/E tRNAs. For some reason it has united the two tRNAs into one molecule, although these are different molecules with different sequences.As the structure contains heterogeneous ...詳細: A/P and P/E tRNAs. For some reason it has united the two tRNAs into one molecule, although these are different molecules with different sequences.As the structure contains heterogeneous population of tRNAs then the identity of tRNA is unknown. 由来: (天然) Rattus norvegicus (ドブネズミ) / 参照: GenBank: 1879656365 |
#82: RNA鎖 | 分子量: 6360.800 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Rattus norvegicus (ドブネズミ) |
+40S ribosomal protein ... , 29種, 29分子 SASBSDSESFSHSISKSLSPSRSSSTSUSVSXSaScSdSCSGSJSMSNSOSWSYSZSb
-タンパク質 , 5種, 5分子 SQSgSeSfn
#12: タンパク質 | 分子量: 16477.377 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Rattus norvegicus (ドブネズミ) / 参照: UniProt: Q5XFV9 |
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#22: 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) Rattus norvegicus (ドブネズミ) / 参照: UniProt: A0A2K6K8B0 |
#33: タンパク質 | 分子量: 6668.938 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Rattus norvegicus (ドブネズミ) / 参照: UniProt: A0A2K6U587 |
#34: タンパク質 | 分子量: 17990.014 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Rattus norvegicus (ドブネズミ) / 参照: UniProt: P62982 |
#74: タンパク質 | 分子量: 14758.394 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Rattus norvegicus (ドブネズミ) / 参照: UniProt: Q6P7R7 |
+60S ribosomal protein ... , 38種, 38分子 ABCFGHIJKLMNPQRTUVWXYZabcdefgh...
-Ribosomal protein ... , 4種, 4分子 OSkp
#49: タンパク質 | 分子量: 24207.285 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Rattus norvegicus (ドブネズミ) / 参照: UniProt: L8Y0W1 |
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#53: タンパク質 | 分子量: 23535.281 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Rattus norvegicus (ドブネズミ) / 参照: UniProt: A0A2J8KH59 |
#71: タンパク質 | 分子量: 11111.032 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Rattus norvegicus (ドブネズミ) / 参照: UniProt: A0A2Y9RW09 |
#76: タンパク質 | 分子量: 12476.973 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Rattus norvegicus (ドブネズミ) / 参照: UniProt: A0A7J7V6K8 |
-タンパク質・ペプチド , 1種, 1分子 y
#84: タンパク質・ペプチド | 分子量: 360.428 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Rattus norvegicus (ドブネズミ) |
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-非ポリマー , 3種, 47分子
#85: 化合物 | ChemComp-MG / #86: 化合物 | ChemComp-ZN / #87: 水 | ChemComp-HOH / | |
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-詳細
研究の焦点であるリガンドがあるか | Y |
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Has protein modification | Y |
-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 |
-試料調製
構成要素 | 名称: Ribosome structure in the rat cortex-hippocampus derived neuronal RNA granules. タイプ: COMPLEX / Entity ID: #1-#79, #82-#84 / 由来: NATURAL | |||||||||||||||||||||||||
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分子量 | 実験値: NO | |||||||||||||||||||||||||
由来(天然) | 生物種: Rattus norvegicus (ドブネズミ) / 器官: Brain / Organelle: RNA granule / 組織: Cortex and hippocampus | |||||||||||||||||||||||||
緩衝液 | pH: 7.5 | |||||||||||||||||||||||||
緩衝液成分 |
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試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES | |||||||||||||||||||||||||
試料支持 | グリッドの材料: COPPER / グリッドのサイズ: 300 divisions/in. / グリッドのタイプ: C-flat-1.2/1.3 | |||||||||||||||||||||||||
急速凍結 | 装置: FEI VITROBOT MARK IV / 凍結剤: ETHANE / 湿度: 100 % / 凍結前の試料温度: 10 K |
-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: OTHER |
電子レンズ | モード: BRIGHT FIELD / 倍率(公称値): 59000 X / 最大 デフォーカス(公称値): 3000 nm / 最小 デフォーカス(公称値): 500 nm / Cs: 2.7 mm / C2レンズ絞り径: 70 µm / アライメント法: COMA FREE |
試料ホルダ | 凍結剤: NITROGEN 試料ホルダーモデル: FEI TITAN KRIOS AUTOGRID HOLDER |
撮影 | 電子線照射量: 30 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) 撮影したグリッド数: 1 / 実像数: 3644 |
-解析
ソフトウェア |
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EMソフトウェア |
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CTF補正 | タイプ: NONE | ||||||||||||||||||||||||||||||||||||||||
粒子像の選択 | 選択した粒子像数: 499054 | ||||||||||||||||||||||||||||||||||||||||
対称性 | 点対称性: C1 (非対称) | ||||||||||||||||||||||||||||||||||||||||
3次元再構成 | 解像度: 2.86 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 62369 / 対称性のタイプ: POINT | ||||||||||||||||||||||||||||||||||||||||
原子モデル構築 | プロトコル: RIGID BODY FIT / 空間: REAL | ||||||||||||||||||||||||||||||||||||||||
原子モデル構築 | PDB-ID: 6OLE Accession code: 6OLE / Source name: PDB / タイプ: experimental model | ||||||||||||||||||||||||||||||||||||||||
精密化 | 交差検証法: NONE 立体化学のターゲット値: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||||||||||||||||||
原子変位パラメータ | Biso mean: 69.49 Å2 | ||||||||||||||||||||||||||||||||||||||||
拘束条件 |
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