Structural highlights
6cfz is a 10 chain structure with sequence from Cbs 144.50 and Chatd. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
|
| Gene: | CTHT_0029740 (CBS 144.50), CTHT_0016520 (CHATD), CTHT_0005680 (CBS 144.50), CTHT_0002350 (CBS 144.50), CTHT_0042930 (CBS 144.50), CTHT_0032660 (CBS 144.50), CTHT_0006450 (CBS 144.50), CTHT_0017540 (CBS 144.50), CTHT_0010600 (CBS 144.50) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Publication Abstract from PubMed
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.
Structure of the DASH/Dam1 complex shows its role at the yeast kinetochore-microtubule interface.,Jenni S, Harrison SC Science. 2018 May 4;360(6388):552-558. doi: 10.1126/science.aar6436. PMID:29724956[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jenni S, Harrison SC. Structure of the DASH/Dam1 complex shows its role at the yeast kinetochore-microtubule interface. Science. 2018 May 4;360(6388):552-558. doi: 10.1126/science.aar6436. PMID:29724956 doi:http://dx.doi.org/10.1126/science.aar6436
