5T58

Structure of the MIND Complex Shows a Regulatory Focus of Yeast Kinetochore Assembly

Summary for 5T58

• Entry DOI: 10.2210/pdb5t58/pdb
• Related: 5T51
• Descriptor: KLLA0F02343p, KLLA0E05809p, KLLA0D15741p, ... (4 entities in total)
• Functional Keywords: cell cycle, kinetochore, complex, chromosome, segregation, mind, mis12, mtw1 complex
• Biological source: Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast); More
• Total number of polymer chains: 4
• Total formula weight: 104274.91

Authors

Dimitrova, Y.,Jenni, S.,Valverde, R.,Khin, Y.,Harrison, S.C. (deposition date: 2016-08-30, release date: 2016-11-09, Last modification date: 2024-03-06)

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

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: 27881300
DOI: 10.1016/j.cell.2016.10.011

Experimental method

X-RAY DIFFRACTION (3.2131 Å)