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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: 8bbf | |||||||||||||||
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タイトル | Structure of the IFT-A complex; IFT-A1 module | |||||||||||||||
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![]() | TRANSPORT PROTEIN / cilia / intraflagellar transport / membrane protein import / complex | |||||||||||||||
機能・相同性 | ![]() smoothened signaling pathway involved in dorsal/ventral neural tube patterning / myotome development / ear morphogenesis / intraciliary anterograde transport / cone photoreceptor outer segment / digestive system development / intraciliary transport particle A / embryonic heart tube left/right pattern formation / embryonic body morphogenesis / neural tube patterning ...smoothened signaling pathway involved in dorsal/ventral neural tube patterning / myotome development / ear morphogenesis / intraciliary anterograde transport / cone photoreceptor outer segment / digestive system development / intraciliary transport particle A / embryonic heart tube left/right pattern formation / embryonic body morphogenesis / neural tube patterning / photoreceptor cell outer segment organization / protein localization to ciliary membrane / intraciliary retrograde transport / establishment of protein localization to organelle / embryonic camera-type eye development / intraciliary transport / gonad development / spinal cord dorsal/ventral patterning / regulation of cilium assembly / photoreceptor connecting cilium / ciliary tip / Intraflagellar transport / camera-type eye morphogenesis / embryonic brain development / non-motile cilium assembly / protein localization to cilium / regulation of smoothened signaling pathway / embryonic heart tube development / embryonic cranial skeleton morphogenesis / non-motile cilium / nervous system process / embryonic forelimb morphogenesis / motile cilium / determination of left/right symmetry / embryonic limb morphogenesis / limb development / embryonic digit morphogenesis / receptor clustering / axoneme / photoreceptor outer segment / cilium assembly / Hedgehog 'off' state / negative regulation of smoothened signaling pathway / centriole / ciliary basal body / neural tube closure / cell morphogenesis / cilium / heart development / protein-containing complex assembly / in utero embryonic development / cytoskeleton / intracellular signal transduction / centrosome / membrane / plasma membrane / cytoplasm 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: 8 Å | |||||||||||||||
![]() | Hesketh, S.J. / Mukhopadhyay, A.G. / Nakamura, D. / Toropova, K. / Roberts, A.J. | |||||||||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: IFT-A structure reveals carriages for membrane protein transport into cilia. 著者: Sophie J Hesketh / Aakash G Mukhopadhyay / Dai Nakamura / Katerina Toropova / Anthony J Roberts / ![]() 要旨: Intraflagellar transport (IFT) trains are massive molecular machines that traffic proteins between cilia and the cell body. Each IFT train is a dynamic polymer of two large complexes (IFT-A and -B) ...Intraflagellar transport (IFT) trains are massive molecular machines that traffic proteins between cilia and the cell body. Each IFT train is a dynamic polymer of two large complexes (IFT-A and -B) and motor proteins, posing a formidable challenge to mechanistic understanding. Here, we reconstituted the complete human IFT-A complex and obtained its structure using cryo-EM. Combined with AlphaFold prediction and genome-editing studies, our results illuminate how IFT-A polymerizes, interacts with IFT-B, and uses an array of β-propeller and TPR domains to create "carriages" of the IFT train that engage TULP adaptor proteins. We show that IFT-A⋅TULP carriages are essential for cilia localization of diverse membrane proteins, as well as ICK-the key kinase regulating IFT train turnaround. These data establish a structural link between IFT-A's distinct functions, provide a blueprint for IFT-A in the train, and shed light on how IFT evolved from a proto-coatomer ancestor. | |||||||||||||||
履歴 |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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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 | ![]() | 442.6 KB | 表示 | ![]() |
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PDB形式 | ![]() | 335.3 KB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
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-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: 153639.297 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() 発現宿主: ![]() ![]() 参照: UniProt: Q8NEZ3 |
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#2: タンパク質 | 分子量: 167328.312 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() 発現宿主: ![]() ![]() 参照: UniProt: Q96RY7 |
#3: タンパク質 | 分子量: 142007.734 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() 発現宿主: ![]() ![]() 参照: UniProt: Q9HBG6 |
-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: IFT-A complex; IFT-A1 module / タイプ: COMPLEX / Entity ID: all / 由来: RECOMBINANT |
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分子量 | 実験値: NO |
由来(天然) | 生物種: ![]() |
由来(組換発現) | 生物種: ![]() ![]() |
緩衝液 | pH: 7.5 |
試料 | 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 IV / 凍結剤: ETHANE |
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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: ![]() |
電子レンズ | モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 3500 nm / 最小 デフォーカス(公称値): 1500 nm |
撮影 | 電子線照射量: 48 e/Å2 フィルム・検出器のモデル: GATAN K3 BIOQUANTUM (6k x 4k) 詳細: Average electron dose for additional dataset was 49.5 (e-/A2) |
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解析
EMソフトウェア | 名称: EPU / カテゴリ: 画像取得 |
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CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION |
3次元再構成 | 解像度: 8 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 136617 / 詳細: Resolution range 7-15A / 対称性のタイプ: POINT |