MOTOR PROTEIN / Kinesin / microtubules / kinesin binding protein / KBP
機能・相同性
機能・相同性情報
transport along microtubule / central nervous system projection neuron axonogenesis / mitochondrion transport along microtubule / kinesin binding / neuron projection maintenance / protein sequestering activity / microtubule cytoskeleton organization / in utero embryonic development / cytoskeleton / mitochondrion 類似検索 - 分子機能
KIF-1 binding protein / KIF-1 binding protein C terminal / Tetratricopeptide-like helical domain superfamily 類似検索 - ドメイン・相同性
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R01GM130556
米国
引用
ジャーナル: Elife / 年: 2020 タイトル: The mechanism of kinesin inhibition by kinesin-binding protein. 著者: Joseph Atherton / Jessica Ja Hummel / Natacha Olieric / Julia Locke / Alejandro Peña / Steven S Rosenfeld / Michel O Steinmetz / Casper C Hoogenraad / Carolyn A Moores / 要旨: Subcellular compartmentalisation is necessary for eukaryotic cell function. Spatial and temporal regulation of kinesin activity is essential for building these local environments via control of ...Subcellular compartmentalisation is necessary for eukaryotic cell function. Spatial and temporal regulation of kinesin activity is essential for building these local environments via control of intracellular cargo distribution. Kinesin-binding protein (KBP) interacts with a subset of kinesins via their motor domains, inhibits their microtubule (MT) attachment, and blocks their cellular function. However, its mechanisms of inhibition and selectivity have been unclear. Here we use cryo-electron microscopy to reveal the structure of KBP and of a KBP-kinesin motor domain complex. KBP is a tetratricopeptide repeat-containing, right-handed α-solenoid that sequesters the kinesin motor domain's tubulin-binding surface, structurally distorting the motor domain and sterically blocking its MT attachment. KBP uses its α-solenoid concave face and edge loops to bind the kinesin motor domain, and selected structure-guided mutations disrupt KBP inhibition of kinesin transport in cells. The KBP-interacting motor domain surface contains motifs exclusively conserved in KBP-interacting kinesins, suggesting a basis for kinesin selectivity.
履歴
登録
2020年7月8日
登録サイト: PDBE / 処理サイト: PDBE
改定 1.0
2020年12月30日
Provider: repository / タイプ: Initial release
改定 1.0
2020年12月30日
Data content type: EM metadata / Data content type: EM metadata / Provider: repository / タイプ: Initial release
改定 1.0
2020年12月30日
Data content type: Image / Data content type: Image / Provider: repository / タイプ: Initial release
改定 1.0
2020年12月30日
Data content type: Primary map / Data content type: Primary map / Provider: repository / タイプ: Initial release
改定 1.0
2020年12月30日
Data content type: Image / Data content type: Image / Provider: repository / タイプ: Initial release
改定 1.0
2020年12月30日
Data content type: Primary map / Data content type: Primary map / Provider: repository / タイプ: Initial release
Data content type: EM metadata / Data content type: EM metadata / EM metadata / Group: Data processing / Experimental summary / Data content type: EM metadata / EM metadata / カテゴリ: em_admin / em_software / Data content type: EM metadata / EM metadata / Item: _em_admin.last_update / _em_software.name
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: Movies were collected with a volta phase plate.Movies were dose weighted.
電子光学装置
位相板: VOLTA PHASE PLATE
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解析
ソフトウェア
名称: PHENIX / バージョン: 1.14_3260: / 分類: 精密化
EMソフトウェア
ID
名称
カテゴリ
8
PHENIX
モデル精密化
11
RELION
最終オイラー角割当
CTF補正
タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION
3次元再構成
解像度: 4.6 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 258049 / 対称性のタイプ: POINT