Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s.
Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s.
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DOI:
10.1038/s41467-018-04044-8
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发表时间:
2018-04-25
影响因子:
16.6
通讯作者:
Sosa H
中科院分区:
文献类型:
--
作者:
Benoit MPMH;Asenjo AB;Sosa H
Kinesin-13s constitute a distinct group within the kinesin superfamily of motor proteins that promote microtubule depolymerization and lack motile activity. The molecular mechanism by which kinesin-13s depolymerize microtubules and are adapted to perform a seemingly very different activity from other kinesins is still unclear. To address this issue, here we report the near atomic resolution cryo-electron microscopy (cryo-EM) structures of Drosophila melanogaster kinesin-13 KLP10A protein constructs bound to curved or straight tubulin in different nucleotide states. These structures show how nucleotide induced conformational changes near the catalytic site are coupled with movement of the kinesin-13-specific loop-2 to induce tubulin curvature leading to microtubule depolymerization. The data highlight a modular structure that allows similar kinesin core motor-domains to be used for different functions, such as motility or microtubule depolymerization. Kinesin-13s are microtubule depolymerases that lack motile activity. Here the authors present the cryo-EM structures of kinesin-13 microtubule complexes in different nucleotide bound states, which reveal how ATP hydrolysis is linked to conformational changes and propose a model for kinesin induced depolymerisation.
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影响因子:
3.4
作者:
Chatterjee, Chandrima;Benoit, Matthieu P. M. H.;Sosa, Hernando
通讯作者:
Sosa, Hernando
影响因子:
16.8
作者:
通讯作者:
--
DOI:
10.1083/jcb.200304034
发表时间:
2003-12-08
期刊:
The Journal of cell biology
影响因子:
--
作者:
Moores CA;Hekmat-Nejad M;Sakowicz R;Milligan RA
通讯作者:
Milligan RA
DOI:
10.1107/s0907444904019158
发表时间:
2004-12-01
影响因子:
2.2
作者:
Emsley, P;Cowtan, K
通讯作者:
Cowtan, K
影响因子:
11.4
作者:
Friel, Claire T.;Howard, Jonathon
通讯作者:
Howard, Jonathon