+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 6qvj | |||||||||||||||||||||
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タイトル | HsCKK (human CAMSAP1) decorated 14pf taxol-GDP microtubule | |||||||||||||||||||||
要素 |
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キーワード | STRUCTURAL PROTEIN / Microtubule CAMSAP Calmodulin-regulated spectrum-associated proteins CKK Cryo-EM Cryo-Electron Microscopy | |||||||||||||||||||||
機能・相同性 | 機能・相同性情報 microtubule minus-end binding / odontoblast differentiation / Post-chaperonin tubulin folding pathway / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Cilium Assembly / Carboxyterminal post-translational modifications of tubulin / Sealing of the nuclear envelope (NE) by ESCRT-III / Intraflagellar transport / cytoskeleton-dependent intracellular transport / Formation of tubulin folding intermediates by CCT/TriC ...microtubule minus-end binding / odontoblast differentiation / Post-chaperonin tubulin folding pathway / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Cilium Assembly / Carboxyterminal post-translational modifications of tubulin / Sealing of the nuclear envelope (NE) by ESCRT-III / Intraflagellar transport / cytoskeleton-dependent intracellular transport / Formation of tubulin folding intermediates by CCT/TriC / Gap junction assembly / COPI-independent Golgi-to-ER retrograde traffic / regulation of cell morphogenesis / Kinesins / Hedgehog 'off' state / Assembly and cell surface presentation of NMDA receptors / GTPase activating protein binding / microtubule organizing center / COPI-dependent Golgi-to-ER retrograde traffic / natural killer cell mediated cytotoxicity / spectrin binding / intercellular bridge / regulation of synapse organization / nuclear envelope lumen / MHC class I protein binding / cytoplasmic microtubule / regulation of microtubule polymerization / Recycling pathway of L1 / microtubule-based process / RHOH GTPase cycle / RHO GTPases activate IQGAPs / spindle assembly / cellular response to interleukin-4 / COPI-mediated anterograde transport / Activation of AMPK downstream of NMDARs / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / cytoskeleton organization / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / Resolution of Sister Chromatid Cohesion / MHC class II antigen presentation / AURKA Activation by TPX2 / Translocation of SLC2A4 (GLUT4) to the plasma membrane / RHO GTPases Activate Formins / PKR-mediated signaling / mitotic spindle / structural constituent of cytoskeleton / microtubule cytoskeleton organization / HCMV Early Events / Aggrephagy / cytoplasmic ribonucleoprotein granule / Separation of Sister Chromatids / The role of GTSE1 in G2/M progression after G2 checkpoint / azurophil granule lumen / microtubule cytoskeleton / Regulation of PLK1 Activity at G2/M Transition / double-stranded RNA binding / neuron projection development / 加水分解酵素; 酸無水物に作用; GTPに作用・細胞または細胞小器官の運動に関与 / mitotic cell cycle / cell body / microtubule binding / microtubule / Potential therapeutics for SARS / cytoskeleton / calmodulin binding / membrane raft / protein domain specific binding / cell division / GTPase activity / ubiquitin protein ligase binding / Neutrophil degranulation / GTP binding / protein-containing complex binding / structural molecule activity / protein-containing complex / extracellular exosome / extracellular region / nucleus / metal ion binding / 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: 3.8 Å | |||||||||||||||||||||
データ登録者 | Atherton, J.M. / Luo, Y. / Xiang, S. / Yang, C. / Jiang, K. / Stangier, M. / Vemu, A. / Cook, A. / Wang, S. / Roll-Mecak, A. ...Atherton, J.M. / Luo, Y. / Xiang, S. / Yang, C. / Jiang, K. / Stangier, M. / Vemu, A. / Cook, A. / Wang, S. / Roll-Mecak, A. / Steinmetz, M.O. / Akhmanova, A. / Baldus, M. / Moores, C.A. | |||||||||||||||||||||
資金援助 | 英国, オランダ, スイス, 6件
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引用 | ジャーナル: Nat Commun / 年: 2019 タイトル: Structural determinants of microtubule minus end preference in CAMSAP CKK domains. 著者: Joseph Atherton / Yanzhang Luo / Shengqi Xiang / Chao Yang / Ankit Rai / Kai Jiang / Marcel Stangier / Annapurna Vemu / Alexander D Cook / Su Wang / Antonina Roll-Mecak / Michel O Steinmetz / ...著者: Joseph Atherton / Yanzhang Luo / Shengqi Xiang / Chao Yang / Ankit Rai / Kai Jiang / Marcel Stangier / Annapurna Vemu / Alexander D Cook / Su Wang / Antonina Roll-Mecak / Michel O Steinmetz / Anna Akhmanova / Marc Baldus / Carolyn A Moores / 要旨: CAMSAP/Patronins regulate microtubule minus-end dynamics. Their end specificity is mediated by their CKK domains, which we proposed recognise specific tubulin conformations found at minus ends. To ...CAMSAP/Patronins regulate microtubule minus-end dynamics. Their end specificity is mediated by their CKK domains, which we proposed recognise specific tubulin conformations found at minus ends. To critically test this idea, we compared the human CAMSAP1 CKK domain (HsCKK) with a CKK domain from Naegleria gruberi (NgCKK), which lacks minus-end specificity. Here we report near-atomic cryo-electron microscopy structures of HsCKK- and NgCKK-microtubule complexes, which show that these CKK domains share the same protein fold, bind at the intradimer interprotofilament tubulin junction, but exhibit different footprints on microtubules. NMR experiments show that both HsCKK and NgCKK are remarkably rigid. However, whereas NgCKK binding does not alter the microtubule architecture, HsCKK remodels its microtubule interaction site and changes the underlying polymer structure because the tubulin lattice conformation is not optimal for its binding. Thus, in contrast to many MAPs, the HsCKK domain can differentiate subtly specific tubulin conformations to enable microtubule minus-end recognition. | |||||||||||||||||||||
履歴 |
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-構造の表示
ムービー |
ムービービューア |
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構造ビューア | 分子: MolmilJmol/JSmol |
-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 6qvj.cif.gz | 332.8 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb6qvj.ent.gz | 268 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 6qvj.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 | 6qvj_validation.pdf.gz | 1.2 MB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 6qvj_full_validation.pdf.gz | 1.3 MB | 表示 | |
XML形式データ | 6qvj_validation.xml.gz | 51.5 KB | 表示 | |
CIF形式データ | 6qvj_validation.cif.gz | 77.8 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/qv/6qvj ftp://data.pdbj.org/pub/pdb/validation_reports/qv/6qvj | HTTPS FTP |
-関連構造データ
-リンク
-集合体
登録構造単位 |
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1 |
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-要素
-タンパク質 , 3種, 5分子 IOXSU
#1: タンパク質 | 分子量: 19628.666 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: CAMSAP1 / 発現宿主: Escherichia coli (大腸菌) / 参照: UniProt: Q5T5Y3 | ||
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#2: タンパク質 | 分子量: 50204.445 Da / 分子数: 2 / 由来タイプ: 天然 / 詳細: GTP / 由来: (天然) Homo sapiens (ヒト) / 細胞株: tsa201 cells / 組織: Embryonic Kidney / 参照: UniProt: P68363 #3: タンパク質 | 分子量: 49717.629 Da / 分子数: 2 / 由来タイプ: 天然 / 詳細: GDP Taxol / 由来: (天然) Homo sapiens (ヒト) / 細胞株: tsa201 / 組織: embryonic kidney / 参照: UniProt: P07437 |
-非ポリマー , 4種, 8分子
#4: 化合物 | #5: 化合物 | #6: 化合物 | #7: 化合物 | |
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-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: FILAMENT / 3次元再構成法: 単粒子再構成法 |
-試料調製
構成要素 |
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由来(天然) |
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由来(組換発現) | 生物種: Escherichia coli (大腸菌) | ||||||||||||||||||||||||
緩衝液 | pH: 6.8 / 詳細: BRB20 | ||||||||||||||||||||||||
試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES | ||||||||||||||||||||||||
急速凍結 | 凍結剤: ETHANE |
-電子顕微鏡撮影
実験機器 | モデル: Tecnai Polara / 画像提供: FEI Company |
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顕微鏡 | モデル: FEI POLARA 300 |
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: 42 e/Å2 / 検出モード: COUNTING フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) 詳細: dose weighted images used in final reconstructions |
-解析
ソフトウェア | 名称: PHENIX / バージョン: 1.11.1_2575: / 分類: 精密化 | |||||||||||||||
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EMソフトウェア |
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CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||||||||
3次元再構成 | 解像度: 3.8 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 33419 / 対称性のタイプ: POINT | |||||||||||||||
原子モデル構築 | プロトコル: OTHER / 空間: REAL |