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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: EMDB / ID: EMD-8001 | |||||||||
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タイトル | RNC in complex with a translocating SecYEG | |||||||||
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![]() | ribosome / translocon | |||||||||
機能・相同性 | ![]() protein insertion into membrane from inner side / cell envelope Sec protein transport complex / intracellular protein transmembrane transport / protein transport by the Sec complex / SRP-dependent cotranslational protein targeting to membrane, translocation / signal sequence binding / stringent response / protein secretion / protein transmembrane transporter activity / transcriptional attenuation ...protein insertion into membrane from inner side / cell envelope Sec protein transport complex / intracellular protein transmembrane transport / protein transport by the Sec complex / SRP-dependent cotranslational protein targeting to membrane, translocation / signal sequence binding / stringent response / protein secretion / protein transmembrane transporter activity / transcriptional attenuation / positive regulation of ribosome biogenesis / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / translational termination / negative regulation of cytoplasmic translation / DnaA-L2 complex / translation repressor activity / negative regulation of DNA-templated DNA replication initiation / mRNA regulatory element binding translation repressor activity / assembly of large subunit precursor of preribosome / ribosome assembly / cytosolic ribosome assembly / response to reactive oxygen species / intracellular protein transport / regulation of cell growth / DNA-templated transcription termination / response to radiation / mRNA 5'-UTR binding / large ribosomal subunit / transferase activity / ribosome binding / 5S rRNA binding / ribosomal large subunit assembly / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / translation / response to antibiotic / negative regulation of DNA-templated transcription / mRNA binding / DNA binding / RNA binding / zinc ion binding / membrane / plasma membrane / cytosol / 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: 3.33 Å | |||||||||
![]() | Jomaa A / Boehringer D | |||||||||
![]() | ![]() タイトル: Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon. 著者: Ahmad Jomaa / Daniel Boehringer / Marc Leibundgut / Nenad Ban / ![]() 要旨: Co-translational protein targeting to membranes is a universally conserved process. Central steps include cargo recognition by the signal recognition particle and handover to the Sec translocon. Here ...Co-translational protein targeting to membranes is a universally conserved process. Central steps include cargo recognition by the signal recognition particle and handover to the Sec translocon. Here we present snapshots of key co-translational-targeting complexes solved by cryo-electron microscopy at near-atomic resolution, establishing the molecular contacts between the Escherichia coli translating ribosome, the signal recognition particle and the translocon. Our results reveal the conformational changes that regulate the latching of the signal sequence, the release of the heterodimeric domains of the signal recognition particle and its receptor, and the handover of the signal sequence to the translocon. We also observe that the signal recognition particle and the translocon insert-specific structural elements into the ribosomal tunnel to remodel it, possibly to sense nascent chains. Our work provides structural evidence for a conformational state of the signal recognition particle and its receptor primed for translocon binding to the ribosome-nascent chain complex. | |||||||||
履歴 |
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構造の表示
ムービー |
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構造ビューア | EMマップ: ![]() ![]() ![]() |
添付画像 |
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マップデータ | ![]() | 116.6 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 47 KB 47 KB | 表示 表示 | ![]() |
画像 | ![]() | 147.6 KB | ||
Filedesc metadata | ![]() | 10.6 KB | ||
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
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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: 1.385 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
CCP4マップ ヘッダ情報:
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-添付データ
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試料の構成要素
+全体 : Ribosome nascent chain SecYEG complex
+超分子 #1: Ribosome nascent chain SecYEG complex
+分子 #1: 23S rRNA
+分子 #2: 5S rRNA
+分子 #36: tRNA CCA end (5'-R(P*CP*CP*A)-3')
+分子 #3: 50S ribosomal protein L2
+分子 #4: 50S ribosomal protein L3
+分子 #5: 50S ribosomal protein L4
+分子 #6: 50S ribosomal protein L5
+分子 #7: 50S ribosomal protein L6
+分子 #8: 50S ribosomal protein L9
+分子 #9: 50S ribosomal protein L10
+分子 #10: 50S ribosomal protein L11
+分子 #11: 50S ribosomal protein L13
+分子 #12: 50S ribosomal protein L14
+分子 #13: 50S ribosomal protein L15
+分子 #14: 50S ribosomal protein L16
+分子 #15: 50S ribosomal protein L17
+分子 #16: 50S ribosomal protein L18
+分子 #17: 50S ribosomal protein L19
+分子 #18: 50S ribosomal protein L20
+分子 #19: 50S ribosomal protein L21
+分子 #20: 50S ribosomal protein L22
+分子 #21: 50S ribosomal protein L23
+分子 #22: 50S ribosomal protein L24
+分子 #23: 50S ribosomal protein L25
+分子 #24: 50S ribosomal protein L27
+分子 #25: 50S ribosomal protein L28
+分子 #26: 50S ribosomal protein L29
+分子 #27: 50S ribosomal protein L30
+分子 #28: 50S ribosomal protein L32
+分子 #29: 50S ribosomal protein L33
+分子 #30: 50S ribosomal protein L34
+分子 #31: 50S ribosomal protein L35
+分子 #32: 50S ribosomal protein L36
+分子 #33: Protein translocase subunit SecY
+分子 #34: Protein translocase subunit SecE
+分子 #35: SecG
+分子 #37: MAGNESIUM ION
+分子 #38: ZINC ION
-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
濃度 | 0.05 mg/mL |
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緩衝液 | pH: 7.5 |
グリッド | モデル: Quantifoil R2/2 / 材質: COPPER / 支持フィルム - 材質: CARBON / 支持フィルム - トポロジー: CONTINUOUS / 前処理 - タイプ: GLOW DISCHARGE / 前処理 - 時間: 30 sec. |
凍結 | 凍結剤: ETHANE / チャンバー内湿度: 100 % / チャンバー内温度: 279 K / 装置: FEI VITROBOT MARK I |
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電子顕微鏡法
顕微鏡 | FEI TITAN KRIOS |
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温度 | 最低: 78.0 K / 最高: 78.0 K |
詳細 | Preliminary grid screening was performed manually. |
撮影 | フィルム・検出器のモデル: FEI FALCON II (4k x 4k) 検出モード: INTEGRATING / 平均電子線量: 20.0 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: ![]() |
電子光学系 | 倍率(補正後): 101083 / 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): 3.5 µm / 最小 デフォーカス(公称値): 1.2 µm / 倍率(公称値): 59000 |
試料ステージ | 試料ホルダーモデル: FEI TITAN KRIOS AUTOGRID HOLDER ホルダー冷却材: NITROGEN |
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |