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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: 5uak | |||||||||
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| タイトル | Dephosphorylated, ATP-free human cystic fibrosis transmembrane conductance regulator (CFTR) | |||||||||
要素 | (Cystic fibrosis transmembrane conductance regulator) x 2 | |||||||||
キーワード | MEMBRANE PROTEIN / HYDROLASE / ABC transporter / anion channel / cystic fibrosis | |||||||||
| 機能・相同性 | 機能・相同性情報positive regulation of voltage-gated chloride channel activity / : / Sec61 translocon complex binding / channel-conductance-controlling ATPase / intracellularly ATP-gated chloride channel activity / positive regulation of enamel mineralization / transepithelial water transport / RHO GTPases regulate CFTR trafficking / amelogenesis / intracellular pH elevation ...positive regulation of voltage-gated chloride channel activity / : / Sec61 translocon complex binding / channel-conductance-controlling ATPase / intracellularly ATP-gated chloride channel activity / positive regulation of enamel mineralization / transepithelial water transport / RHO GTPases regulate CFTR trafficking / amelogenesis / intracellular pH elevation / chloride channel inhibitor activity / : / multicellular organismal-level water homeostasis / Golgi-associated vesicle membrane / cholesterol transport / bicarbonate transport / bicarbonate transmembrane transporter activity / chloride channel regulator activity / membrane hyperpolarization / vesicle docking involved in exocytosis / chloride transmembrane transporter activity / sperm capacitation / cholesterol biosynthetic process / RHOQ GTPase cycle / chloride channel activity / positive regulation of exocytosis / ATPase-coupled transmembrane transporter activity / chloride channel complex / positive regulation of insulin secretion involved in cellular response to glucose stimulus / ABC-type transporter activity / 14-3-3 protein binding / cellular response to forskolin / chloride transmembrane transport / response to endoplasmic reticulum stress / cellular response to cAMP / PDZ domain binding / establishment of localization in cell / clathrin-coated endocytic vesicle membrane / Defective CFTR causes cystic fibrosis / Late endosomal microautophagy / recycling endosome / ABC-family proteins mediated transport / transmembrane transport / recycling endosome membrane / Chaperone Mediated Autophagy / Aggrephagy / Cargo recognition for clathrin-mediated endocytosis / protein-folding chaperone binding / Clathrin-mediated endocytosis / early endosome membrane / early endosome / endosome membrane / Ub-specific processing proteases / apical plasma membrane / lysosomal membrane / endoplasmic reticulum membrane / enzyme binding / cell surface / ATP hydrolysis activity / protein-containing complex / ATP binding / nucleus / membrane / plasma membrane / cytosol / cytoplasm 類似検索 - 分子機能 | |||||||||
| 生物種 | Homo sapiens (ヒト) | |||||||||
| 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: 3.87 Å | |||||||||
データ登録者 | Liu, F. / Zhang, Z. / Chen, J. | |||||||||
引用 | ジャーナル: Cell / 年: 2017タイトル: Molecular Structure of the Human CFTR Ion Channel. 著者: Fangyu Liu / Zhe Zhang / László Csanády / David C Gadsby / Jue Chen / ![]() 要旨: The cystic fibrosis transmembrane conductance regulator (CFTR) is an ATP-binding cassette (ABC) transporter that uniquely functions as an ion channel. Here, we present a 3.9 Å structure of ...The cystic fibrosis transmembrane conductance regulator (CFTR) is an ATP-binding cassette (ABC) transporter that uniquely functions as an ion channel. Here, we present a 3.9 Å structure of dephosphorylated human CFTR without nucleotides, determined by electron cryomicroscopy (cryo-EM). Close resemblance of this human CFTR structure to zebrafish CFTR under identical conditions reinforces its relevance for understanding CFTR function. The human CFTR structure reveals a previously unresolved helix belonging to the R domain docked inside the intracellular vestibule, precluding channel opening. By analyzing the sigmoid time course of CFTR current activation, we propose that PKA phosphorylation of the R domain is enabled by its infrequent spontaneous disengagement, which also explains residual ATPase and gating activity of dephosphorylated CFTR. From comparison with MRP1, a feature distinguishing CFTR from all other ABC transporters is the helix-loop transition in transmembrane helix 8, which likely forms the structural basis for CFTR's channel function. | |||||||||
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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 | 5uak.cif.gz | 243.9 KB | 表示 | PDBx/mmCIF形式 |
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| PDB形式 | pdb5uak.ent.gz | 191.2 KB | 表示 | PDB形式 |
| PDBx/mmJSON形式 | 5uak.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 | 5uak_validation.pdf.gz | 838.4 KB | 表示 | wwPDB検証レポート |
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| 文書・詳細版 | 5uak_full_validation.pdf.gz | 839.4 KB | 表示 | |
| XML形式データ | 5uak_validation.xml.gz | 33.6 KB | 表示 | |
| CIF形式データ | 5uak_validation.cif.gz | 51.1 KB | 表示 | |
| アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/ua/5uak ftp://data.pdbj.org/pub/pdb/validation_reports/ua/5uak | 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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| 1 |
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要素
| #1: タンパク質 | 分子量: 169353.578 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: CFTR, ABCC7 / 細胞株 (発現宿主): HEK293S GnTI- / 発現宿主: Homo sapiens (ヒト) / 参照: UniProt: P13569, EC: 3.6.3.49 |
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| #2: タンパク質・ペプチド | 分子量: 1635.006 Da / 分子数: 1 / Fragment: R domain / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: CFTR, ABCC7 / 細胞株 (発現宿主): HEK293S GnTI- / 発現宿主: Homo sapiens (ヒト) |
-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 | 名称: human cystic fibrosis transmembrane conductance regulator (CFTR) タイプ: COMPLEX / Entity ID: all / 由来: RECOMBINANT |
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| 分子量 | 値: 168 kDa/nm / 実験値: NO |
| 由来(天然) | 生物種: Homo sapiens (ヒト) |
| 由来(組換発現) | 生物種: Homo sapiens (ヒト) / 細胞: HEK293S GnTI- / プラスミド: BacMam |
| 緩衝液 | pH: 7.5 |
| 試料 | 濃度: 5 mg/ml / 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
| 急速凍結 | 装置: FEI VITROBOT MARK I / 凍結剤: ETHANE / 湿度: 100 % / 凍結前の試料温度: 298 K |
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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 |
| 電子銃 | 電子線源: FIELD EMISSION GUN / 加速電圧: 300 kV / 照射モード: FLOOD BEAM |
| 電子レンズ | モード: BRIGHT FIELD |
| 撮影 | 電子線照射量: 1.68 e/Å2 フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) |
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解析
| CTF補正 | タイプ: NONE |
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| 3次元再構成 | 解像度: 3.87 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 415915 / 対称性のタイプ: POINT |
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万見について




Homo sapiens (ヒト)
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UCSF Chimera












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