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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: PDB / ID: 3jc2 | ||||||
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| タイトル | The structure of the mammalian Sec61 channel opened by a signal sequence | ||||||
要素 |
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キーワード | TRANSPORT PROTEIN / Sec61 / translocation / signal sequence | ||||||
| 機能・相同性 | 機能・相同性情報long-day photoperiodism / response to external biotic stimulus / positive regulation of biosynthetic process / prolactin receptor binding / peptide hormone secretion / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / membrane docking / positive regulation of lactation / pronephric nephron development / response to L-arginine ...long-day photoperiodism / response to external biotic stimulus / positive regulation of biosynthetic process / prolactin receptor binding / peptide hormone secretion / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / membrane docking / positive regulation of lactation / pronephric nephron development / response to L-arginine / regulation of meiotic cell cycle process involved in oocyte maturation / cotranslational protein targeting to membrane / Ssh1 translocon complex / Sec61 translocon complex / protein targeting to ER / protein insertion into ER membrane / SRP-dependent cotranslational protein targeting to membrane, translocation / positive regulation of fatty acid biosynthetic process / signal sequence binding / mammary gland development / post-translational protein targeting to membrane, translocation / blastocyst formation / biosynthetic process / response to food / positive regulation of endocytosis / protein transmembrane transporter activity / response to mechanical stimulus / lactation / positive regulation of phagocytosis / positive regulation of receptor signaling pathway via JAK-STAT / response to nutrient levels / female pregnancy / positive regulation of non-canonical NF-kappaB signal transduction / hormone activity / phospholipid binding / positive regulation of nitric oxide biosynthetic process / ribosome binding / cell surface receptor signaling pathway / positive regulation of canonical NF-kappaB signal transduction / endoplasmic reticulum lumen / inflammatory response / negative regulation of gene expression / positive regulation of gene expression / endoplasmic reticulum membrane / negative regulation of apoptotic process / extracellular space / extracellular region / metal ion binding / cytosol 類似検索 - 分子機能 | ||||||
| 生物種 | ![]() ![]() | ||||||
| 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: 3.6 Å | ||||||
データ登録者 | Voorhees, R.M. / Hegde, R.S. | ||||||
引用 | ジャーナル: Science / 年: 2016タイトル: Structure of the Sec61 channel opened by a signal sequence. 著者: Rebecca M Voorhees / Ramanujan S Hegde / ![]() 要旨: Secreted and integral membrane proteins compose up to one-third of the biological proteome. These proteins contain hydrophobic signals that direct their translocation across or insertion into the ...Secreted and integral membrane proteins compose up to one-third of the biological proteome. These proteins contain hydrophobic signals that direct their translocation across or insertion into the lipid bilayer by the Sec61 protein-conducting channel. The molecular basis of how hydrophobic signals within a nascent polypeptide trigger channel opening is not understood. Here, we used cryo-electron microscopy to determine the structure of an active Sec61 channel that has been opened by a signal sequence. The signal supplants helix 2 of Sec61α, which triggers a rotation that opens the central pore both axially across the membrane and laterally toward the lipid bilayer. Comparisons with structures of Sec61 in other states suggest a pathway for how hydrophobic signals engage the channel to gain access to the lipid bilayer. | ||||||
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構造の表示
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| 構造ビューア | 分子: Molmil Jmol/JSmol |
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ダウンロードとリンク
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ダウンロード
| PDBx/mmCIF形式 | 3jc2.cif.gz | 110.1 KB | 表示 | PDBx/mmCIF形式 |
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| PDB形式 | pdb3jc2.ent.gz | 85 KB | 表示 | PDB形式 |
| PDBx/mmJSON形式 | 3jc2.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 | 3jc2_validation.pdf.gz | 795.2 KB | 表示 | wwPDB検証レポート |
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| 文書・詳細版 | 3jc2_full_validation.pdf.gz | 807.5 KB | 表示 | |
| XML形式データ | 3jc2_validation.xml.gz | 23.3 KB | 表示 | |
| CIF形式データ | 3jc2_validation.cif.gz | 33.3 KB | 表示 | |
| アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/jc/3jc2 ftp://data.pdbj.org/pub/pdb/validation_reports/jc/3jc2 | HTTPS FTP |
-関連構造データ
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リンク
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集合体
| 登録構造単位 | ![]()
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要素
| #1: タンパク質 | 分子量: 52279.379 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: purified from native canine microsomes / 由来: (天然) ![]() |
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| #2: タンパク質 | 分子量: 7019.456 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: purified from native canine microsomes / 由来: (天然) ![]() |
| #3: タンパク質・ペプチド | 分子量: 2053.576 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() Tissue fraction (発現宿主): reticulocyte translation extract in the presence of canine microsomes 参照: UniProt: Q6VMP1, UniProt: P01239*PLUS |
| #4: タンパク質・ペプチド | 分子量: 2741.370 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: purified from native canine microsomes / 由来: (天然) ![]() |
| Has protein modification | N |
-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 |
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試料調製
| 構成要素 |
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| 緩衝液 | 名称: 50 mM HEPES, 200 mM potassium acetate, 15 mM magnesium acetate, 1 mM DTT, 0.25% Digitonin pH: 7.5 詳細: 50 mM HEPES, 200 mM potassium acetate, 15 mM magnesium acetate, 1 mM DTT, 0.25% Digitonin | ||||||||||||||||||||||||
| 試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES | ||||||||||||||||||||||||
| 試料支持 | 詳細: Quantifoil (R2/2) holey carbon grid covered in a 70 Angstrom-thick layer of amorphous carbon | ||||||||||||||||||||||||
| 急速凍結 | 装置: FEI VITROBOT MARK I / 凍結剤: ETHANE / 湿度: 100 % 詳細: 3 uL sample was added to the grid, incubated for 30 seconds at 4 C, blotted for 9 seconds, and then plunged into liquid ethane (FEI VITROBOT). 手法: 3 uL sample was added to the grid, incubated for 30 seconds at 4 C, blotted for 9 seconds |
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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 / 日付: 2015年3月6日 |
| 電子銃 | 電子線源: FIELD EMISSION GUN / 加速電圧: 300 kV / 照射モード: SPOT SCAN |
| 電子レンズ | モード: BRIGHT FIELD / 倍率(公称値): 59000 X / 倍率(補正後): 104478 X / 最大 デフォーカス(公称値): 3500 nm / 最小 デフォーカス(公称値): 2000 nm |
| 撮影 | 電子線照射量: 27 e/Å2 フィルム・検出器のモデル: FEI FALCON II (4k x 4k) |
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解析
| EMソフトウェア |
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| 対称性 | 点対称性: C1 (非対称) | |||||||||||||||||||||
| 3次元再構成 | 解像度: 3.6 Å / 粒子像の数: 101339 / ピクセルサイズ(公称値): 1.34 Å / ピクセルサイズ(実測値): 1.34 Å / 対称性のタイプ: POINT | |||||||||||||||||||||
| 原子モデル構築 | 空間: REAL / Target criteria: R-factor 詳細: DETAILS--Real-space fitting using Chimera and Coot followed by reciprocal-space refinement using REFMAC | |||||||||||||||||||||
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| 精密化ステップ | サイクル: LAST
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万見について






引用
UCSF Chimera








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