6b0l
From Proteopedia
KLP10A-AMPPNP in complex with a microtubule
Structural highlights
Function[TBA1B_PIG] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. [KI10A_DROME] Required during anaphase to drive sister chromatid separation to promote flux by actively depolymerizing kinetochore microtubules at their pole-associated minus ends, thereby moving chromatids through a "poleward flux".[1] [F2Z5B2_PIG] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.[RuleBase:RU003505] Publication Abstract from PubMedKinesin-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. Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s.,Benoit MPMH, Asenjo AB, Sosa H Nat Commun. 2018 Apr 25;9(1):1662. doi: 10.1038/s41467-018-04044-8. PMID:29695795[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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