2ZFL

Crystal Structure of the Kif1A Motor Domain during Mg release: Mg-releasing Transition-3

2ZFL の概要

• エントリーDOI: 10.2210/pdb2zfl/pdb
• 関連するPDBエントリー: 1I5S 1I6I 1VFV 1VFW 1VFX 1VFZ 2ZFI 2ZFJ 2ZFK 2ZFM
• 分子名称: Kinesin-like protein KIF1A, Kinesin heavy chain isoform 5C, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: kinesin, alpha and beta protein, enzyme, atpase, p-loop, motor protein, atp-binding, coiled coil, microtubule, nucleotide-binding, transport protein
• 由来する生物種: Mus musculus (Mouse); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton : P28738
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41555.42

構造登録者

Nitta, R.,Okada, Y.,Hirokawa, N. (登録日: 2008-01-08, 公開日: 2008-09-23, 最終更新日: 2023-11-01)

主引用文献

Nitta, R.,Okada, Y.,Hirokawa, N.
Structural model for strain-dependent microtubule activation of Mg-ADP release from kinesin.
Nat.Struct.Mol.Biol., 15:1067-1075, 2008

PubMed Abstract: Mg-ADP release is considered to be a crucial process for the regulation and motility of kinesin. To gain insight into the structural basis of this process, we solved the atomic structures of kinesin superfamily protein-1A (KIF1A) during and after Mg(2+) release. On the basis of new structural and mutagenesis data, we propose a model mechanism for microtubule activation of Mg-ADP release from KIF1A. In our model, a specific interaction between loop L7 of KIF1A and beta-tubulin reconfigures the KIF1A active site by shifting the relative positions of switches I and II. This leads to the sequential release of a group of water molecules that sits over the Mg(2+) in the active site, followed by Mg(2+) and finally the ADP. We further propose that this set of events is linked to a strain-dependent docking of the neck linker to the motor core, which produces a two-step power stroke.

PubMed: 18806800
DOI: 10.1038/nsmb.1487

実験手法

X-RAY DIFFRACTION (2.7 Å)