4UXT

Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins

4UXT の概要

• エントリーDOI: 10.2210/pdb4uxt/pdb
• 関連するPDBエントリー: 4UXO 4UXP 4UXR 4UXS 4UXY 4UY0
• EMDBエントリー: 2769
• 分子名称: TUBULIN ALPHA-1B CHAIN, TUBULIN BETA-2B CHAIN, KINESIN HEAVY CHAIN ISOFORM 5A, ... (8 entities in total)
• 機能のキーワード: transport protein
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton: P81947 Q6B856; Cytoplasm, perinuclear region : Q12840
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 139955.19

構造登録者

Atherton, J.,Farabella, I.,Yu, I.M.,Rosenfeld, S.S.,Houdusse, A.,Topf, M.,Moores, C. (登録日: 2014-08-27, 公開日: 2014-09-24, 最終更新日: 2024-05-08)

主引用文献

Atherton, J.,Farabella, I.,Yu, I.,Rosenfeld, S.S.,Houdusse, A.,Topf, M.,Moores, C.A.
Conserved Mechanisms of Microtubule-Stimulated Adp Release, ATP Binding, and Force Generation in Transport Kinesins.
Elife, 3:3680-, 2014

PubMed Abstract: Kinesins are a superfamily of microtubule-based ATP-powered motors, important for multiple, essential cellular functions. How microtubule binding stimulates their ATPase and controls force generation is not understood. To address this fundamental question, we visualized microtubule-bound kinesin-1 and kinesin-3 motor domains at multiple steps in their ATPase cycles--including their nucleotide-free states--at ∼ 7 Å resolution using cryo-electron microscopy. In both motors, microtubule binding promotes ordered conformations of conserved loops that stimulate ADP release, enhance microtubule affinity and prime the catalytic site for ATP binding. ATP binding causes only small shifts of these nucleotide-coordinating loops but induces large conformational changes elsewhere that allow force generation and neck linker docking towards the microtubule plus end. Family-specific differences across the kinesin-microtubule interface account for the distinctive properties of each motor. Our data thus provide evidence for a conserved ATP-driven mechanism for kinesins and reveal the critical mechanistic contribution of the microtubule interface.

PubMed: 25209998
DOI: 10.7554/ELIFE.03680

実験手法

ELECTRON MICROSCOPY (7.4 Å)