2P4N

Human Monomeric Kinesin (1BG2) and Bovine Tubulin (1JFF) Docked into the 9-Angstrom Cryo-EM Map of Nucleotide-Free Kinesin Complexed to the Microtubule

2P4N の概要

• エントリーDOI: 10.2210/pdb2p4n/pdb
• 関連するPDBエントリー: 1BG2 1JFF
• EMDBエントリー: 1340
• 分子名称: Kinesin heavy chain, Tubulin alpha chain, Tubulin beta chain, ... (9 entities in total)
• 機能のキーワード: motor protein, atpase, transport protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 138795.61

構造登録者

Sindelar, C.V.,Downing, K.H. (登録日: 2007-03-12, 公開日: 2008-07-08, 最終更新日: 2024-02-21)

主引用文献

Sindelar, C.V.,Downing, K.H.
The beginning of kinesin's force-generating cycle visualized at 9-A resolution.
J.Cell Biol., 177:377-385, 2007

PubMed Abstract: We have used cryo-electron microscopy of kinesin-decorated microtubules to resolve the structure of the motor protein kinesin's crucial nucleotide response elements, switch I and the switch II helix, in kinesin's poorly understood nucleotide-free state. Both of the switch elements undergo conformational change relative to the microtubule-free state. The changes in switch I suggest a role for it in "ejecting" adenosine diphosphate when kinesin initially binds to the microtubule. The switch II helix has an N-terminal extension, apparently stabilized by conserved microtubule contacts, implying a microtubule activation mechanism that could convey the state of the bound nucleotide to kinesin's putative force-delivering element (the "neck linker"). In deriving this structure, we have adapted an image-processing technique, single-particle reconstruction, for analyzing decorated microtubules. The resulting reconstruction visualizes the asymmetric seam present in native, 13-protofilament microtubules, and this method will provide an avenue to higher-resolution characterization of a variety of microtubule- binding proteins, as well as the microtubule itself.

PubMed: 17470637
DOI: 10.1083/jcb.200612090

実験手法

ELECTRON MICROSCOPY (9 Å)