Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7KDF

Structure of Stu2 Bound to dwarf Ndc80c

Summary for 7KDF
Entry DOI10.2210/pdb7kdf/pdb
DescriptorNDC80 isoform 1,NDC80 isoform 1, NUF2 isoform 1,NUF2 isoform 1, Spc24, ... (7 entities in total)
Functional Keywordsstu2, tension sensing, ndc80, kinetochore, cell cycle
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
More
Total number of polymer chains5
Total formula weight87174.69
Authors
Zahm, J.A.,Stewart, M.G.,Miller, M.P.,Harrison, S.C. (deposition date: 2020-10-08, release date: 2020-11-11, Last modification date: 2024-11-06)
Primary citationZahm, J.A.,Stewart, M.G.,Carrier, J.S.,Harrison, S.C.,Miller, M.P.
Structural basis of Stu2 recruitment to yeast kinetochores.
Elife, 10:-, 2021
Cited by
PubMed Abstract: Chromosome segregation during cell division requires engagement of kinetochores of sister chromatids with microtubules emanating from opposite poles. As the corresponding microtubules shorten, these 'bioriented' sister kinetochores experience tension-dependent stabilization of microtubule attachments. The yeast XMAP215 family member and microtubule polymerase, Stu2, associates with kinetochores and contributes to tension-dependent stabilization in vitro. We show here that a C-terminal segment of Stu2 binds the four-way junction of the Ndc80 complex (Ndc80c) and that residues conserved both in yeast Stu2 orthologs and in their metazoan counterparts make specific contacts with Ndc80 and Spc24. Mutations that perturb this interaction prevent association of Stu2 with kinetochores, impair cell viability, produce biorientation defects, and delay cell cycle progression. Ectopic tethering of the mutant Stu2 species to the Ndc80c junction restores wild-type function in vivo. These findings show that the role of Stu2 in tension-sensing depends on its association with kinetochores by binding with Ndc80c.
PubMed: 33591274
DOI: 10.7554/eLife.65389
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.72 Å)
Structure validation

231029

PDB entries from 2025-02-05

PDB statisticsPDBj update infoContact PDBjnumon