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データを開く
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基本情報
登録情報 | ![]() | |||||||||
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タイトル | Cryo-EM structure of ribosome-Sec61 in complex with cyclotriazadisulfonamide derivative CK147 | |||||||||
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機能・相同性 | ![]() regulation of G1 to G0 transition / exit from mitosis / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / regulation of translation involved in cellular response to UV / protein-DNA complex disassembly / positive regulation of DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator / optic nerve development / retinal ganglion cell axon guidance / G1 to G0 transition / positive regulation of signal transduction by p53 class mediator ...regulation of G1 to G0 transition / exit from mitosis / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / regulation of translation involved in cellular response to UV / protein-DNA complex disassembly / positive regulation of DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator / optic nerve development / retinal ganglion cell axon guidance / G1 to G0 transition / positive regulation of signal transduction by p53 class mediator / ubiquitin ligase inhibitor activity / protein transmembrane transporter activity / protein-RNA complex assembly / protein targeting / negative regulation of ubiquitin-dependent protein catabolic process / cellular response to actinomycin D / rough endoplasmic reticulum / DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest / maturation of LSU-rRNA / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosomal large subunit biogenesis / positive regulation of translation / cellular response to gamma radiation / transcription coactivator binding / mRNA 5'-UTR binding / rRNA processing / antimicrobial humoral immune response mediated by antimicrobial peptide / ribosome binding / retina development in camera-type eye / regulation of translation / 5S rRNA binding / large ribosomal subunit rRNA binding / defense response to Gram-negative bacterium / cytosolic large ribosomal subunit / killing of cells of another organism / cytoplasmic translation / tRNA binding / postsynaptic density / protein stabilization / rRNA binding / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / mRNA binding / positive regulation of cell population proliferation / ubiquitin protein ligase binding / synapse / endoplasmic reticulum membrane / positive regulation of gene expression / nucleolus / negative regulation of transcription by RNA polymerase II / endoplasmic reticulum / RNA binding / nucleoplasm / nucleus / metal ion binding / cytoplasm 類似検索 - 分子機能 | |||||||||
生物種 | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 2.79 Å | |||||||||
![]() | Pauwels E / Shewakramani NR / De Wijngaert B / Vermeire K / Das K | |||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Structural insights into TRAP association with ribosome-Sec61 complex and translocon inhibition by a CADA derivative. 著者: Eva Pauwels / Neesha R Shewakramani / Brent De Wijngaert / Anita Camps / Becky Provinciael / Joren Stroobants / Kai-Uwe Kalies / Enno Hartmann / Piet Maes / Kurt Vermeire / Kalyan Das / ![]() ![]() 要旨: During cotranslational translocation, the signal peptide of a nascent chain binds Sec61 translocon to initiate protein transport through the endoplasmic reticulum (ER) membrane. Our cryo-electron ...During cotranslational translocation, the signal peptide of a nascent chain binds Sec61 translocon to initiate protein transport through the endoplasmic reticulum (ER) membrane. Our cryo-electron microscopy structure of ribosome-Sec61 shows binding of an ordered heterotetrameric translocon-associated protein (TRAP) complex, in which TRAP-γ is anchored at two adjacent positions of 28 ribosomal RNA and interacts with ribosomal protein L38 and Sec61α/γ. Four transmembrane helices (TMHs) of TRAP-γ cluster with one C-terminal helix of each α, β, and δ subunits. The seven TMH bundle helps position a crescent-shaped trimeric TRAP-α/β/δ core in the ER lumen, facing the Sec61 channel. Further, our in vitro assay establishes the cyclotriazadisulfonamide derivative CK147 as a translocon inhibitor. A structure of ribosome-Sec61-CK147 reveals CK147 binding the channel and interacting with the plug helix from the lumenal side. The CK147 resistance mutations surround the inhibitor. These structures help in understanding the TRAP functions and provide a new Sec61 site for designing translocon inhibitors. | |||||||||
履歴 |
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構造の表示
添付画像 |
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ダウンロードとリンク
-EMDBアーカイブ
マップデータ | ![]() | 96.6 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 64.8 KB 64.8 KB | 表示 表示 | ![]() |
FSC (解像度算出) | ![]() | 12.4 KB | 表示 | ![]() |
画像 | ![]() | 56 KB | ||
その他 | ![]() ![]() | 131.6 MB 131.6 MB | ||
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 | ![]() 8b6cMC ![]() 8b5lC M: このマップから作成された原子モデル 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
EMDBのページ | ![]() ![]() |
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「今月の分子」の関連する項目 |
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マップ
ファイル | ![]() | ||||||||||||||||||||||||||||||||||||
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投影像・断面図 | 画像のコントロール
画像は Spider により作成 | ||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 1.23 Å | ||||||||||||||||||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
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-添付データ
-ハーフマップ: #2
ファイル | emd_15863_half_map_1.map | ||||||||||||
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投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: #1
ファイル | emd_15863_half_map_2.map | ||||||||||||
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投影像・断面図 |
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密度ヒストグラム |
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試料の構成要素
+全体 : 80S ribosome complex with Sec61 and inhibitor CK147
+超分子 #1: 80S ribosome complex with Sec61 and inhibitor CK147
+分子 #1: 60S ribosomal protein L21
+分子 #3: 60S ribosomal protein L7
+分子 #4: Ribosomal_L18_c domain-containing protein
+分子 #5: 60S ribosomal protein L18a
+分子 #6: 60S ribosomal protein L29
+分子 #7: Ribosomal protein L3
+分子 #8: 60S ribosomal protein L31
+分子 #10: 60S ribosomal protein L7a
+分子 #11: 60S ribosomal protein L11
+分子 #12: 60S ribosomal protein L30
+分子 #13: Ribosomal protein L37
+分子 #14: Ribosomal protein L8
+分子 #15: Ribosomal protein L10
+分子 #16: Protein transport protein Sec61 subunit gamma
+分子 #17: 60S ribosomal protein L37a
+分子 #18: 60S ribosomal protein L23
+分子 #19: 60S ribosomal protein L40
+分子 #20: 60S ribosomal protein L39-like
+分子 #21: 60S ribosomal protein L17
+分子 #22: 60S ribosomal protein L6
+分子 #23: eL18
+分子 #24: 60S ribosomal protein L19
+分子 #25: Ribosomal protein L24
+分子 #26: 60S ribosomal protein L13a
+分子 #27: Protein transport protein Sec61 subunit alpha isoform 1
+分子 #28: 60S ribosomal protein L4
+分子 #29: 60S ribosomal protein L36a-like
+分子 #30: 60S ribosomal protein L28
+分子 #31: 60S ribosomal protein L35a
+分子 #32: Ribosomal protein L32
+分子 #33: 60S ribosomal protein L27
+分子 #34: 60S ribosomal protein L27a
+分子 #35: 60S ribosomal protein L34
+分子 #36: 60S ribosomal protein L38
+分子 #37: 60S ribosomal protein L9
+分子 #38: 60S ribosomal protein L13
+分子 #40: Ribosomal protein L15
+分子 #41: 60S ribosomal protein L36
+分子 #42: 60S ribosomal protein L35
+分子 #43: 60S ribosomal protein L14
+分子 #44: Ribosomal protein L26
+分子 #45: Ribosomal_L23eN domain-containing protein
+分子 #46: 60S ribosomal protein L22 (Fragment)
+分子 #47: 60S ribosomal protein L41
+分子 #2: 28S rRNA
+分子 #9: 5.8S rRNA
+分子 #39: 5S rRNA
+分子 #48: MAGNESIUM ION
+分子 #49: ZINC ION
+分子 #50: 4-[[9-(cyclohexylmethyl)-3-methylidene-5-(4-methylphenyl)sulfonyl...
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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![]() | 単粒子再構成法 |
試料の集合状態 | particle |
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試料調製
緩衝液 | pH: 7.5 |
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グリッド | モデル: Quantifoil R1.2/1.3 / 材質: COPPER / メッシュ: 300 / 支持フィルム - 材質: CARBON / 支持フィルム - トポロジー: HOLEY / 支持フィルム - Film thickness: 2.0 nm / 前処理 - タイプ: GLOW DISCHARGE / 前処理 - 時間: 30 sec. / 前処理 - 雰囲気: AIR / 前処理 - 気圧: 0.015 kPa |
凍結 | 凍結剤: ETHANE / チャンバー内湿度: 95 % / チャンバー内温度: 277.15 K / 装置: FEI VITROBOT MARK IV |
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電子顕微鏡法
顕微鏡 | TFS GLACIOS |
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撮影 | フィルム・検出器のモデル: FEI FALCON III (4k x 4k) 検出モード: COUNTING / 撮影したグリッド数: 1 / 実像数: 1734 / 平均露光時間: 40.0 sec. / 平均電子線量: 0.8 e/Å2 |
電子線 | 加速電圧: 200 kV / 電子線源: ![]() |
電子光学系 | C2レンズ絞り径: 50.0 µm / 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / Cs: 2.7 mm / 最大 デフォーカス(公称値): 1.8 µm / 最小 デフォーカス(公称値): 0.6 µm / 倍率(公称値): 120000 |
試料ステージ | 試料ホルダーモデル: OTHER / ホルダー冷却材: NITROGEN |