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基本情報
登録情報 | データベース: EMDB / ID: EMD-3617 | |||||||||
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タイトル | Quaternary complex between SRP, SR, and SecYEG bound to the translating ribosome | |||||||||
![]() | 'Quaternary structure of the SRP, SR, SecYEG, and the translating ribosome' | |||||||||
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![]() | Ribosome / SRP / Sec translocon / SRP receptor / quaternary complex | |||||||||
機能・相同性 | ![]() protein insertion into membrane from inner side / cell envelope Sec protein transport complex / signal recognition particle binding / signal recognition particle / intracellular protein transmembrane transport / protein transport by the Sec complex / signal-recognition-particle GTPase / protein-transporting ATPase activity / SRP-dependent cotranslational protein targeting to membrane, translocation / 7S RNA binding ...protein insertion into membrane from inner side / cell envelope Sec protein transport complex / signal recognition particle binding / signal recognition particle / intracellular protein transmembrane transport / protein transport by the Sec complex / signal-recognition-particle GTPase / protein-transporting ATPase activity / SRP-dependent cotranslational protein targeting to membrane, translocation / 7S RNA binding / signal sequence binding / SRP-dependent cotranslational protein targeting to membrane / protein targeting to membrane / stringent response / protein secretion / protein transmembrane transporter activity / transcriptional attenuation / positive regulation of ribosome biogenesis / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / protein targeting / 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 / cytoplasmic side of plasma membrane / 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 / ribonucleoprotein complex / response to antibiotic / negative regulation of DNA-templated transcription / GTPase activity / mRNA binding / GTP binding / protein homodimerization activity / ATP hydrolysis activity / 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: 4.8 Å | |||||||||
![]() | Jomaa A / Hwang Fu Y | |||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome. 著者: Ahmad Jomaa / Yu-Hsien Hwang Fu / Daniel Boehringer / Marc Leibundgut / Shu-Ou Shan / Nenad Ban / ![]() ![]() 要旨: During co-translational protein targeting, the signal recognition particle (SRP) binds to the translating ribosome displaying the signal sequence to deliver it to the SRP receptor (SR) on the ...During co-translational protein targeting, the signal recognition particle (SRP) binds to the translating ribosome displaying the signal sequence to deliver it to the SRP receptor (SR) on the membrane, where the signal peptide is transferred to the translocon. Using electron cryo-microscopy, we have determined the structure of a quaternary complex of the translating Escherichia coli ribosome, the SRP-SR in the 'activated' state and the translocon. Our structure, supported by biochemical experiments, reveals that the SRP RNA adopts a kinked and untwisted conformation to allow repositioning of the 'activated' SRP-SR complex on the ribosome. In addition, we observe the translocon positioned through interactions with the SR in the vicinity of the ribosome exit tunnel where the signal sequence is extending beyond its hydrophobic binding groove of the SRP M domain towards the translocon. Our study provides new insights into the mechanism of signal sequence transfer from the SRP to the translocon. | |||||||||
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CIF形式データ | ![]() | 7.6 KB | 表示 | |
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「今月の分子」の関連する項目 |
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ファイル | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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注釈 | 'Quaternary structure of the SRP, SR, SecYEG, and the translating ribosome' | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: 1.39 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, SRP, SR, and SecYEG quaternary complex
+超分子 #1: Ribosome nascent chain, SRP, SR, and SecYEG quaternary complex
+超分子 #2: Ribosome
+超分子 #3: SRP, SR, and SecYEG
+分子 #1: 4.5S SRP RNA (Ffs)
+分子 #2: P-site tRNA-CCA end
+分子 #3: 23S rRNA
+分子 #4: 5S rRNA
+分子 #5: 50S ribosomal protein L2
+分子 #6: 50S ribosomal protein L3
+分子 #7: 50S ribosomal protein L4
+分子 #8: 50S ribosomal protein L5
+分子 #9: 50S ribosomal protein L6
+分子 #10: 50S ribosomal protein L9
+分子 #11: 50S ribosomal protein L10
+分子 #12: 50S ribosomal protein L11
+分子 #13: 50S ribosomal protein L13
+分子 #14: 50S ribosomal protein L14
+分子 #15: 50S ribosomal protein L15
+分子 #16: 50S ribosomal protein L16
+分子 #17: 50S ribosomal protein L17
+分子 #18: 50S ribosomal protein L18
+分子 #19: 50S ribosomal protein L19
+分子 #20: 50S ribosomal protein L20
+分子 #21: 50S ribosomal protein L21
+分子 #22: 50S ribosomal protein L22
+分子 #23: 50S ribosomal protein L23
+分子 #24: 50S ribosomal protein L24
+分子 #25: 50S ribosomal protein L25
+分子 #26: 50S ribosomal protein L27
+分子 #27: 50S ribosomal protein L28
+分子 #28: 50S ribosomal protein L29
+分子 #29: 50S ribosomal protein L30
+分子 #30: 50S ribosomal protein L32
+分子 #31: 50S ribosomal protein L33
+分子 #32: 50S ribosomal protein L34
+分子 #33: 50S ribosomal protein L35
+分子 #34: 50S ribosomal protein L36
+分子 #35: Protein translocase subunit SecY
+分子 #36: Protein translocase subunit SecE
+分子 #37: Signal recognition particle protein,Signal recognition particle p...
+分子 #38: Protein-export membrane protein SecG
+分子 #39: Signal sequence (1A9L)
+分子 #40: Signal recognition particle receptor FtsY
+分子 #41: ZINC ION
+分子 #42: TETRAFLUOROALUMINATE ION
+分子 #43: MAGNESIUM ION
+分子 #44: GUANOSINE-5'-DIPHOSPHATE
-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 | 0.1 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 / メッシュ: 200 / 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: 277 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: 85.0 K |
撮影 | フィルム・検出器のモデル: FEI FALCON II (4k x 4k) 検出モード: OTHER / 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): 100719 / 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / Cs: 2.7 mm |
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 |
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画像解析
-原子モデル構築 1
精密化 | 空間: RECIPROCAL / プロトコル: RIGID BODY FIT 当てはまり具合の基準: Cross-correlation coefficient |
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得られたモデル | ![]() PDB-5nco: |