National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R01GM113164
United States
Citation
Journal: Nat Commun / Year: 2018 Title: Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s. Authors: Matthieu P M H Benoit / Ana B Asenjo / Hernando Sosa / Abstract: 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- ...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.
History
Deposition
Sep 14, 2017
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Header (metadata) release
Nov 1, 2017
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Map release
May 2, 2018
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Update
Mar 13, 2024
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Current status
Mar 13, 2024
Processing site: RCSB / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Name: microtubule / type: organelle_or_cellular_component / ID: 3 / Parent: 1 / Macromolecule list: #2, #1 Details: Chains A and B make up a curved microtubule protofilament.
Source (natural)
Organism: Sus scrofa (pig)
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Macromolecule #1: Tubulin alpha-1B chain
Macromolecule
Name: Tubulin alpha-1B chain / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
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