6CFZ

Structure of the DASH/Dam1 complex shows its role at the yeast kinetochore-microtubule interface

Summary for 6CFZ

• Entry DOI: 10.2210/pdb6cfz/pdb
• EMDB information: 7446 7469
• Descriptor: Ask1, Spc34, Dad3, ... (10 entities in total)
• Functional Keywords: dash, dam1 complex, ask1, dad1, dad2, dad3, dad4, dam1, duo1, hsk3, spc19, spc34, kinetochore, kinetochore-microtubule interface, chromosome segregation, cell-division, point-centromere yeast, nuclear protein
• Biological source: Chaetomium thermophilum; More
• Total number of polymer chains: 10
• Total formula weight: 116148.55

Authors

Jenni, S.,Harrison, S.C. (deposition date: 2018-02-19, release date: 2018-05-02, Last modification date: 2024-03-13)

Primary citation

Jenni, S.,Harrison, S.C.
Structure of the DASH/Dam1 complex shows its role at the yeast kinetochore-microtubule interface.
Science, 360:552-558, 2018

PubMed Abstract: Kinetochores connect mitotic-spindle microtubules with chromosomes, allowing microtubule depolymerization to pull chromosomes apart during anaphase while resisting detachment as the microtubule shortens. The heterodecameric DASH/Dam1 complex (DASH/Dam1c), an essential component of yeast kinetochores, assembles into a microtubule-encircling ring. The ring associates with rodlike Ndc80 complexes to organize the kinetochore-microtubule interface. We report the cryo-electron microscopy structure (at ~4.5-angstrom resolution) of a DASH/Dam1c ring and a molecular model of its ordered components, validated by evolutionary direct-coupling analysis. Integrating this structure with that of the Ndc80 complex and with published interaction data yields a molecular picture of kinetochore-microtubule attachment, including how flexible, C-terminal extensions of DASH/Dam1c subunits project and contact widely separated sites on the Ndc80 complex rod and how phosphorylation at previously identified sites might regulate kinetochore assembly.

PubMed: 29724956
DOI: 10.1126/science.aar6436

Experimental method

ELECTRON MICROSCOPY (4.5 Å)