3LRE
Crystal Structure Analysis of Human Kinesin-8 Motor Domain
3LRE の概要
エントリーDOI | 10.2210/pdb3lre/pdb |
分子名称 | Kinesin-like protein KIF18A, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
機能のキーワード | motor protein, nucleotide binding, microtubule binding, atp-binding, cell projection, cytoskeleton, glycoprotein, microtubule, nucleotide-binding, nucleus, phosphoprotein, protein transport, transport |
由来する生物種 | Homo sapiens (human) |
細胞内の位置 | Cell projection, ruffle: Q8NI77 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 80479.52 |
構造登録者 | |
主引用文献 | Peters, C.,Brejc, K.,Belmont, L.,Bodey, A.J.,Lee, Y.,Yu, M.,Guo, J.,Sakowicz, R.,Hartman, J.,Moores, C.A. Insight into the molecular mechanism of the multitasking kinesin-8 motor. Embo J., 29:3437-3447, 2010 Cited by PubMed Abstract: Members of the kinesin-8 motor class have the remarkable ability to both walk towards microtubule plus-ends and depolymerise these ends on arrival, thereby regulating microtubule length. To analyse how kinesin-8 multitasks, we studied the structure and function of the kinesin-8 motor domain. We determined the first crystal structure of a kinesin-8 and used cryo-electron microscopy to calculate the structure of the microtubule-bound motor. Microtubule-bound kinesin-8 reveals a new conformation compared with the crystal structure, including a bent conformation of the α4 relay helix and ordering of functionally important loops. The kinesin-8 motor domain does not depolymerise stabilised microtubules with ATP but does form tubulin rings in the presence of a non-hydrolysable ATP analogue. This shows that, by collaborating, kinesin-8 motor domain molecules can release tubulin from microtubules, and that they have a similar mechanical effect on microtubule ends as kinesin-13, which enables depolymerisation. Our data reveal aspects of the molecular mechanism of kinesin-8 motors that contribute to their unique dual motile and depolymerising functions, which are adapted to control microtubule length. PubMed: 20818331DOI: 10.1038/emboj.2010.220 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.2 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード
