5MU3

Crystal structure of Ctf19-Mcm21 kinetochore assembly bound with Ctf19-Mcm21 binding motif of central kinetochore subunit Okp1

Summary for 5MU3

• Entry DOI: 10.2210/pdb5mu3/pdb
• Related: 3ZXU
• Descriptor: Central kinetochore subunit MCM21, Central kinetochore subunit CTF19, Central kinetochore subunit Okp1, ... (5 entities in total)
• Functional Keywords: cell cycle, chromosome segregation, centromere, kinetochore, rwd domain
• Biological source: Kluyveromyces lactis NRRL Y-1140; More
• Total number of polymer chains: 6
• Total formula weight: 97484.03

Authors

Schmitzberger, F. (deposition date: 2017-01-12, release date: 2017-11-01, Last modification date: 2024-01-17)

Primary citation

Schmitzberger, F.,Richter, M.M.,Gordiyenko, Y.,Robinson, C.V.,Dadlez, M.,Westermann, S.
Molecular basis for inner kinetochore configuration through RWD domain-peptide interactions.
EMBO J., 36:3458-3482, 2017

PubMed Abstract: Kinetochores are dynamic cellular structures that connect chromosomes to microtubules. They form from multi-protein assemblies that are evolutionarily conserved between yeasts and humans. One of these assemblies-COMA-consists of subunits Ame1, Ctf19, Mcm21 and Okp1 A description of COMA molecular organization has so far been missing. We defined the subunit topology of COMA, bound with inner kinetochore proteins Nkp1 and Nkp2, from the yeast , with nanoflow electrospray ionization mass spectrometry, and mapped intermolecular contacts with hydrogen-deuterium exchange coupled to mass spectrometry. Our data suggest that the essential Okp1 subunit is a multi-segmented nexus with distinct binding sites for Ame1, Nkp1-Nkp2 and Ctf19-Mcm21. Our crystal structure of the Ctf19-Mcm21 RWD domains bound with Okp1 shows the molecular contacts of this important inner kinetochore joint. The Ctf19-Mcm21 binding motif in Okp1 configures a branch of mitotic inner kinetochores, by tethering Ctf19-Mcm21 and Chl4-Iml3 Absence of this motif results in dependence on the mitotic checkpoint for viability.

PubMed: 29046335
DOI: 10.15252/embj.201796636

Experimental method

X-RAY DIFFRACTION (2.1 Å)