3ZFD

Crystal Structure of the Kif4 Motor Domain Complexed With Mg-AMPPNP

3ZFD の概要

• エントリーDOI: 10.2210/pdb3zfd/pdb
• 関連するPDBエントリー: 3ZFC
• 分子名称: CHROMOSOME-ASSOCIATED KINESIN KIF4, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• 機能のキーワード: hydrolase, molecular motor, atpase, microtubule
• 由来する生物種: MUS MUSCULUS (HOUSE MOUSE)
• 細胞内の位置: Nucleus: P33174
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39598.87

構造登録者

Chang, Q.,Nitta, R.,Inoue, S.,Hirokawa, N. (登録日: 2012-12-11, 公開日: 2013-03-20, 最終更新日: 2023-12-20)

主引用文献

Chang, Q.,Nitta, R.,Inoue, S.,Hirokawa, N.
Structural Basis for the ATP-Induced Isomerization of Kinesin.
J.Mol.Biol., 425:1869-, 2013

PubMed Abstract: Kinesin superfamily proteins (KIFs) are microtubule-based molecular motors driven by the energy derived from the hydrolysis of ATP. Previous studies have revealed that the ATP binding step is crucial both for the power stroke to produce motility and for the inter-domain regulation of ATPase activity to guarantee the processive movement of dimeric KIFs. Here, we report the first crystal structure of KIF4 complexed with the non-hydrolyzable ATP analog, AMPPNP (adenylyl imidodiphosphate), at 1.7Å resolution. By combining our structure with previously solved KIF1A structures complexed with two ATP analogs, molecular snapshots during ATP binding reveal that the closure of the nucleotide-binding pocket during ATP binding is achieved by closure of the backdoor. Closure of the backdoor stabilizes two mobile regions, switch I and switch II, to generate the phosphate tube from which hydrolyzed phosphate is released. Through the stabilization of switch II, the local conformational change at the catalytic center is further relayed to the neck-linker element that fully docks to the catalytic core to produce the power stroke. Because the neck linker is a sole element that connects the partner heads in dimeric KIFs, this tight structural coordination between the catalytic center and neck linker enables inter-domain communication between the partner heads. This study also revealed the putative microtubule-binding site of KIF4, thus providing structural insights that describe the specific binding of KIF4 to the microtubule.

PubMed: 23500491
DOI: 10.1016/J.JMB.2013.03.004

実験手法

X-RAY DIFFRACTION (1.71 Å)