EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	An atomic-level mechanism for activation of the kinesin molecular motors.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 107, Issue 9, Page 4111-4116, Year 2010
掲載日	2010年3月2日
著者	Charles V Sindelar / Kenneth H Downing /
PubMed 要旨	Kinesin cytoskeletal motors convert the energy of ATP hydrolysis into stepping movement along microtubules. A partial model of this process has been derived from crystal structures, which show that ...Kinesin cytoskeletal motors convert the energy of ATP hydrolysis into stepping movement along microtubules. A partial model of this process has been derived from crystal structures, which show that movement of the motor domain relative to its major microtubule binding element, the switch II helix, is coupled to docking of kinesin's neck linker element along the motor domain. This docking would displace the cargo in the direction of travel and so contribute to a step. However, the crystal structures do not reveal how ATP binding and hydrolysis govern this series of events. We used cryoelectron microscopy to derive 8-9 A-resolution maps of four nucleotide states encompassing the microtubule-attached kinetic cycle of a kinesin motor. The exceptionally high quality of these maps allowed us to build in crystallographically determined conformations of kinesin's key subcomponents, yielding novel arrangements of kinesin's switch II helix and nucleotide-sensing switch loops. The resulting atomic models reveal a seesaw mechanism in which the switch loops, triggered by ATP binding, propel their side of the motor domain down and thereby elicit docking of the neck linker on the opposite side of the seesaw. Microtubules engage the seesaw mechanism by stabilizing the formation of extra turns at the N terminus of the switch II helix, which then serve as an anchor for the switch loops as they modulate the seesaw angle. These observations explain how microtubules activate kinesin's ATP-sensing machinery to promote cargo displacement and inform the mechanism of kinesin's ancestral relative, myosin.
リンク	Proc Natl Acad Sci U S A / PubMed:20160108 / PubMed Central
手法	EM (らせん対称)
解像度	8.5 - 9.1 Å
構造データ	EMDB-5164: 3D reconstruction a microtubule decorated with monomeric human kinesin (K349 construct) in complex with ADP. 手法: EM (らせん対称) / 解像度: 9.1 Å EMDB-5165: 3D reconstruction a microtubule decorated with monomeric human kinesin (K349 construct) having an empty nucleotide pocket. 手法: EM (らせん対称) / 解像度: 8.5 Å EMDB-5166: 3D reconstruction of a microtubule decorated with monomeric human kinesin (K349 construct) having AMPPNP bound in the nucleotide pocket. 手法: EM (らせん対称) / 解像度: 9.1 Å EMDB-5167: 3D reconstruction of a microtubule decorated with monomeric human kinesin (K349 construct) having ADP aluminum fluoride complex bound in the nucleotide pocket. 手法: EM (らせん対称) / 解像度: 9.1 Å
由来	unidentified (未定義)