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基本情報
登録情報 | データベース: PDB / ID: 3j2u | ||||||
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タイトル | Kinesin-13 KLP10A HD in complex with CS-tubulin and a microtubule | ||||||
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![]() | MOTOR PROTEIN / tubulin / kinesin / kinesin-13 / KinI / depolymerase / depolymerization / microtubule / Kinesin13 | ||||||
機能・相同性 | ![]() establishment of mitotic spindle asymmetry / establishment of meiotic spindle orientation / plus-end specific microtubule depolymerization / asymmetric protein localization involved in cell fate determination / cortical microtubule / meiotic spindle pole / mitotic spindle astral microtubule / centriole assembly / COPI-dependent Golgi-to-ER retrograde traffic / Kinesins ...establishment of mitotic spindle asymmetry / establishment of meiotic spindle orientation / plus-end specific microtubule depolymerization / asymmetric protein localization involved in cell fate determination / cortical microtubule / meiotic spindle pole / mitotic spindle astral microtubule / centriole assembly / COPI-dependent Golgi-to-ER retrograde traffic / Kinesins / mitotic chromosome movement towards spindle pole / kinetochore microtubule / meiotic spindle organization / spindle assembly involved in female meiosis I / non-motile cilium assembly / plus-end-directed microtubule motor activity / meiotic spindle / positive regulation of axon guidance / microtubule depolymerization / microtubule motor activity / kinesin complex / spindle organization / microtubule-based movement / mitotic spindle pole / cytoskeletal motor activity / centrosome duplication / microtubule-based process / chromosome, centromeric region / mitotic spindle organization / 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 / structural constituent of cytoskeleton / spindle pole / microtubule cytoskeleton organization / spindle / microtubule cytoskeleton / mitotic cell cycle / nervous system development / microtubule binding / microtubule / protein heterodimerization activity / cell division / GTPase activity / centrosome / GTP binding / ATP hydrolysis activity / ATP binding / metal ion binding / cytosol / cytoplasm 類似検索 - 分子機能 | ||||||
生物種 | ![]() ![]() ![]() ![]() | ||||||
手法 | 電子顕微鏡法 / らせん対称体再構成法 / クライオ電子顕微鏡法 / 解像度: 10.8 Å | ||||||
![]() | Asenjo, A.B. / Chatterjee, C. / Tan, D. / DePaoli, V. / Rice, W.J. / Diaz-Avalos, R. / Silvestry, M. / Sosa, H. | ||||||
![]() | ![]() タイトル: Structural model for tubulin recognition and deformation by kinesin-13 microtubule depolymerases. 著者: Ana B Asenjo / Chandrima Chatterjee / Dongyan Tan / Vania DePaoli / William J Rice / Ruben Diaz-Avalos / Mariena Silvestry / Hernando Sosa / ![]() 要旨: To elucidate the structural basis of the mechanism of microtubule depolymerization by kinesin-13s, we analyzed complexes of tubulin and the Drosophila melanogaster kinesin-13 KLP10A by electron ...To elucidate the structural basis of the mechanism of microtubule depolymerization by kinesin-13s, we analyzed complexes of tubulin and the Drosophila melanogaster kinesin-13 KLP10A by electron microscopy (EM) and fluorescence polarization microscopy. We report a nanometer-resolution (1.1 nm) cryo-EM three-dimensional structure of the KLP10A head domain (KLP10AHD) bound to curved tubulin. We found that binding of KLP10AHD induces a distinct tubulin configuration with displacement (shear) between tubulin subunits in addition to curvature. In this configuration, the kinesin-binding site differs from that in straight tubulin, providing an explanation for the distinct interaction modes of kinesin-13s with the microtubule lattice or its ends. The KLP10AHD-tubulin interface comprises three areas of interaction, suggesting a crossbow-type tubulin-bending mechanism. These areas include the kinesin-13 family conserved KVD residues, and as predicted from the crossbow model, mutating these residues changes the orientation and mobility of KLP10AHDs interacting with the microtubule. | ||||||
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構造の表示
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構造ビューア | 分子: ![]() ![]() |
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PDBx/mmCIF形式 | ![]() | 393 KB | 表示 | ![]() |
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PDB形式 | ![]() | 312.8 KB | 表示 | ![]() |
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その他 | ![]() |
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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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対称性 | らせん対称: (回転対称性: 1 / Dyad axis: no / N subunits divisor: 1 / Num. of operations: 42 / Rise per n subunits: 5.553 Å / Rotation per n subunits: 168.087 °) |
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要素
#1: タンパク質 | 分子量: 41810.918 Da / 分子数: 1 / 断片: head domain (UNP residues 279-615) / 由来タイプ: 組換発現 由来: (組換発現) ![]() ![]() 遺伝子: Klp10A, CG1453 / 発現宿主: ![]() ![]() | ||
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#2: タンパク質 | 分子量: 50107.238 Da / 分子数: 2 / 由来タイプ: 天然 / 由来: (天然) ![]() ![]() #3: タンパク質 | 分子量: 49907.770 Da / 分子数: 2 / 由来タイプ: 天然 / 由来: (天然) ![]() ![]() |
-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: らせん対称体再構成法 |
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試料調製
構成要素 | 名称: kinesin-13 KLP10A head domain in complex with CS-tubulin and a microtubule タイプ: COMPLEX |
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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 I / 凍結剤: ETHANE |
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電子顕微鏡撮影
実験機器 | ![]() モデル: Tecnai F20 / 画像提供: FEI Company | |||||||||||||||
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EM imaging | 日付: 2012年5月1日 / 電子線源:
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解析
EMソフトウェア |
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CTF補正 | 詳細: each particle | ||||||||||||||||||||||||
らせん対称 | 回転角度/サブユニット: 168.087 ° / 軸方向距離/サブユニット: 5.553 Å / らせん対称軸の対称性: C1 | ||||||||||||||||||||||||
3次元再構成 | 解像度: 10.8 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 54584 / ピクセルサイズ(公称値): 2 Å / ピクセルサイズ(実測値): 2 Å / Refinement type: HALF-MAPS REFINED INDEPENDENTLY / 対称性のタイプ: HELICAL | ||||||||||||||||||||||||
原子モデル構築 | プロトコル: RIGID BODY FIT / 空間: REAL 詳細: REFINEMENT PROTOCOL--RIGID BODY DETAILS--The domains were separately fitted with the global fitting option of the routine fitmap within UCSF-Chimera. Best fit was chosen based on the maximum ...詳細: REFINEMENT PROTOCOL--RIGID BODY DETAILS--The domains were separately fitted with the global fitting option of the routine fitmap within UCSF-Chimera. Best fit was chosen based on the maximum cross-correlation value between the EM density and an 11 A resolution density model of the atomic structure of the domain to be fitted. | ||||||||||||||||||||||||
原子モデル構築 | 3D fitting-ID: 1 / Accession code: 1JFF / Initial refinement model-ID: 1 / PDB-ID: 1JFF / Source name: PDB / タイプ: experimental model
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精密化ステップ | サイクル: LAST
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