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基本情報
登録情報 | データベース: EMDB / ID: EMD-11774 | |||||||||
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タイトル | Cryo-EM structure of the signal sequence-engaged post-translational Sec translocon | |||||||||
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![]() | Post-translational translocation / Protein translocation / Sec complex / Signal sequence / MEMBRANE PROTEIN | |||||||||
機能・相同性 | ![]() mating pheromone activity / mating / misfolded protein transport / Sec62/Sec63 complex / translocon complex / pheromone-dependent signal transduction involved in conjugation with cellular fusion / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / cytosol to endoplasmic reticulum transport / protein transmembrane import into intracellular organelle / rough endoplasmic reticulum membrane ...mating pheromone activity / mating / misfolded protein transport / Sec62/Sec63 complex / translocon complex / pheromone-dependent signal transduction involved in conjugation with cellular fusion / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / cytosol to endoplasmic reticulum transport / protein transmembrane import into intracellular organelle / rough endoplasmic reticulum membrane / Ssh1 translocon complex / Sec61 translocon complex / protein-transporting ATPase activity / filamentous growth / post-translational protein targeting to endoplasmic reticulum membrane / SRP-dependent cotranslational protein targeting to membrane / signal sequence binding / SRP-dependent cotranslational protein targeting to membrane, translocation / post-translational protein targeting to membrane, translocation / cupric ion binding / peptide transmembrane transporter activity / nuclear inner membrane / retrograde protein transport, ER to cytosol / protein transmembrane transporter activity / ERAD pathway / guanyl-nucleotide exchange factor activity / cell periphery / ribosome binding / endoplasmic reticulum membrane / structural molecule activity / endoplasmic reticulum / mitochondrion / RNA binding / extracellular region / membrane / cytosol 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: 4.4 Å | |||||||||
![]() | Weng T-H / Beatrix B | |||||||||
![]() | ![]() タイトル: Architecture of the active post-translational Sec translocon. 著者: Tsai-Hsuan Weng / Wieland Steinchen / Birgitta Beatrix / Otto Berninghausen / Thomas Becker / Gert Bange / Jingdong Cheng / Roland Beckmann / ![]() 要旨: In eukaryotes, most secretory and membrane proteins are targeted by an N-terminal signal sequence to the endoplasmic reticulum, where the trimeric Sec61 complex serves as protein-conducting channel ...In eukaryotes, most secretory and membrane proteins are targeted by an N-terminal signal sequence to the endoplasmic reticulum, where the trimeric Sec61 complex serves as protein-conducting channel (PCC). In the post-translational mode, fully synthesized proteins are recognized by a specialized channel additionally containing the Sec62, Sec63, Sec71, and Sec72 subunits. Recent structures of this Sec complex in the idle state revealed the overall architecture in a pre-opened state. Here, we present a cryo-EM structure of the yeast Sec complex bound to a substrate, and a crystal structure of the Sec62 cytosolic domain. The signal sequence is inserted into the lateral gate of Sec61α similar to previous structures, yet, with the gate adopting an even more open conformation. The signal sequence is flanked by two Sec62 transmembrane helices, the cytoplasmic N-terminal domain of Sec62 is more rigidly positioned, and the plug domain is relocated. We crystallized the Sec62 domain and mapped its interaction with the C-terminus of Sec63. Together, we obtained a near-complete and integrated model of the active Sec complex. | |||||||||
履歴 |
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構造の表示
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構造ビューア | EMマップ: ![]() ![]() ![]() |
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マップデータ | ![]() | 28.2 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 26.8 KB 26.8 KB | 表示 表示 | ![]() |
FSC (解像度算出) | ![]() | 7.2 KB | 表示 | ![]() |
画像 | ![]() | 51.9 KB | ||
Filedesc metadata | ![]() | 7.6 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: 1.059 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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試料の構成要素
+全体 : Signal sequence-engaged post-translational Sec translocon
+超分子 #1: Signal sequence-engaged post-translational Sec translocon
+超分子 #2: Signal sequence-engaged post-translational Sec translocon
+超分子 #3: Translocation protein SEC62
+超分子 #4: Mating factor alpha-1
+分子 #1: Protein transport protein SEC61
+分子 #2: Protein transport protein SBH1
+分子 #3: Protein transport protein SSS1
+分子 #4: Protein translocation protein SEC63
+分子 #5: Translocation protein SEC66
+分子 #6: Translocation protein SEC72
+分子 #7: Translocation protein SEC62,Translocation protein SEC62
+分子 #8: Mating factor alpha-1,Mating factor alpha-1
-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 | 5 mg/mL | ||||||||||||||||||
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緩衝液 | pH: 7.4 構成要素:
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グリッド | モデル: UltrAuFoil R2/2 / 材質: GOLD | ||||||||||||||||||
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 IV |
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電子顕微鏡法
顕微鏡 | FEI TITAN KRIOS |
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撮影 | #0 - Image recording ID: 1 #0 - フィルム・検出器のモデル: GATAN K2 QUANTUM (4k x 4k) #0 - 検出モード: COUNTING / #0 - 撮影したグリッド数: 1 / #0 - 平均電子線量: 36.0 e/Å2 / #1 - Image recording ID: 2 #1 - フィルム・検出器のモデル: GATAN K2 QUANTUM (4k x 4k) #1 - 検出モード: COUNTING / #1 - 撮影したグリッド数: 1 / #1 - 平均電子線量: 48.0 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: ![]() |
電子光学系 | 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD |
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |