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-Structure paper
タイトル | Insight into the molecular mechanism of the multitasking kinesin-8 motor. |
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ジャーナル・号・ページ | EMBO J, Vol. 29, Issue 20, Page 3437-3447, Year 2010 |
掲載日 | 2010年10月20日 |
著者 | Carsten Peters / Katjuša Brejc / Lisa Belmont / Andrew J Bodey / Yan Lee / Ming Yu / Jun Guo / Roman Sakowicz / James Hartman / Carolyn A Moores / |
PubMed 要旨 | 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 ...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. |
リンク | EMBO J / PubMed:20818331 / PubMed Central |
手法 | EM (らせん対称) / X線回折 |
解像度 | 2.2 - 13.0 Å |
構造データ | EMDB-1701: EMDB-1702: PDB-3lre: |
化合物 | ChemComp-MG: ChemComp-ADP: ChemComp-HOH: |
由来 |
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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 |