6B0L

KLP10A-AMPPNP in complex with a microtubule

Summary for 6B0L

• Entry DOI: 10.2210/pdb6b0l/pdb
• EMDB information: 7026 7027 7028
• Descriptor: Tubulin alpha-1B chain, Tubulin beta chain, Kinesin-like protein Klp10A, ... (8 entities in total)
• Functional Keywords: kinesin 13, microtubule, tubulin, depolymerization, motor protein-structural protein complex, motor protein/structural protein
• Biological source: Drosophila melanogaster (Fruit fly); More
• Total number of polymer chains: 3
• Total formula weight: 149555.18

Authors

Benoit, M.P.M.H.,Asenjo, A.B.,Sosa, H. (deposition date: 2017-09-14, release date: 2018-05-02, Last modification date: 2024-03-13)

Primary citation

Benoit, M.P.M.H.,Asenjo, A.B.,Sosa, H.
Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s.
Nat Commun, 9:1662-1662, 2018

PubMed 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-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.

PubMed: 29695795
DOI: 10.1038/s41467-018-04044-8

Experimental method

ELECTRON MICROSCOPY (3.98 Å)