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8G0Q

Crystal structure of the yeast Ndc80:Nuf2 head region with a bound Dam1 segment

Summary for 8G0Q
Entry DOI10.2210/pdb8g0q/pdb
DescriptorKinetochore protein NDC80, DASH complex subunit DAM1,Kinetochore protein NUF2 (2 entities in total)
Functional Keywordscell division, chromosome segregation, kinetochore, ndc80 complex, ndc80, nuf2, dam1, dash-dam1 complex, phospho-regulation, cell cycle
Biological sourceSaccharomyces cerevisiae (baker's yeast)
More
Total number of polymer chains4
Total formula weight122035.06
Authors
Zahm, J.A.,Jenni, S.,Harrison, S.C. (deposition date: 2023-02-01, release date: 2023-03-29, Last modification date: 2024-05-22)
Primary citationZahm, J.A.,Jenni, S.,Harrison, S.C.
Structure of the Ndc80 complex and its interactions at the yeast kinetochore-microtubule interface.
Open Biology, 13:220378-220378, 2023
Cited by
PubMed Abstract: The conserved Ndc80 kinetochore complex, Ndc80c, is the principal link between mitotic spindle microtubules and centromere-associated proteins. We used AlphaFold 2 (AF2) to obtain predictions of the Ndc80 'loop' structure and of the Ndc80 : Nuf2 globular head domains that interact with the Dam1 subunit of the heterodecameric DASH/Dam1 complex (Dam1c). The predictions guided design of crystallizable constructs, with structures close to the predicted ones. The Ndc80 'loop' is a stiff, α-helical 'switchback' structure; AF2 predictions and positions of preferential cleavage sites indicate that flexibility within the long Ndc80c rod occurs instead at a hinge closer to the globular head. Conserved stretches of the Dam1 C terminus bind Ndc80c such that phosphorylation of Dam1 serine residues 257, 265 and 292 by the mitotic kinase Ipl1/Aurora B can release this contact during error correction of mis-attached kinetochores. We integrate the structural results presented here into our current molecular model of the kinetochore-microtubule interface. The model illustrates how multiple interactions between Ndc80c, DASH/Dam1c and the microtubule lattice stabilize kinetochore attachments.
PubMed: 36883282
DOI: 10.1098/rsob.220378
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.22 Å)
Structure validation

237735

数据于2025-06-18公开中

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