5T6J
Structure of the MIND Complex Shows a Regulatory Focus of Yeast Kinetochore Assembly
Summary for 5T6J
Entry DOI | 10.2210/pdb5t6j/pdb |
Descriptor | Kinetochore protein SPC24, Kinetochore protein SPC25, Kinetochore-associated protein DSN1, ... (4 entities in total) |
Functional Keywords | cell cycle, kinetochore, complex, chromosome, segregation, mind, mis12, mtw1, spc24, spc25, ndc80, nuf2 |
Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
Cellular location | Nucleus : Q04477 P40014 P40568 |
Total number of polymer chains | 3 |
Total formula weight | 18424.03 |
Authors | Valverde, R.,Jenni, S.,Dimitrova, Y.,Khin, Y.,Harrison, S.C. (deposition date: 2016-09-01, release date: 2016-11-09, Last modification date: 2023-10-04) |
Primary citation | Dimitrova, Y.N.,Jenni, S.,Valverde, R.,Khin, Y.,Harrison, S.C. Structure of the MIND Complex Defines a Regulatory Focus for Yeast Kinetochore Assembly. Cell, 167:1014-1027.e12, 2016 Cited by PubMed Abstract: Kinetochores connect centromeric nucleosomes with mitotic-spindle microtubules through conserved, cross-interacting protein subassemblies. In budding yeast, the heterotetrameric MIND complex (Mtw1, Nnf1, Nsl1, Dsn1), ortholog of the metazoan Mis12 complex, joins the centromere-proximal components, Mif2 and COMA, with the principal microtubule-binding component, the Ndc80 complex (Ndc80C). We report the crystal structure of Kluyveromyces lactis MIND and examine its partner interactions, to understand the connection from a centromeric nucleosome to a much larger microtubule. MIND resembles an elongated, asymmetric Y; two globular heads project from a coiled-coil shaft. An N-terminal extension of Dsn1 from one head regulates interactions of the other head, blocking binding of Mif2 and COMA. Dsn1 phosphorylation by Ipl1/Aurora B relieves this autoinhibition, enabling MIND to join an assembling kinetochore. A C-terminal extension of Dsn1 recruits Ndc80C to the opposite end of the shaft. The structure and properties of MIND show how it integrates phospho-regulatory inputs for kinetochore assembly and disassembly. PubMed: 27881300DOI: 10.1016/j.cell.2016.10.011 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.752 Å) |
Structure validation
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