7QOO

Structure of the human inner kinetochore CCAN complex

Summary for 7QOO

• Entry DOI: 10.2210/pdb7qoo/pdb
• EMDB information: 14098
• Descriptor: Centromere protein C, Centromere protein U, Centromere protein Q, ... (15 entities in total)
• Functional Keywords: inner kinetochore, ccan, complex, dna binding protein, cell cycle
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 15
• Total formula weight: 544716.80

Authors

Vetter, I.R.,Pesenti, M.,Raisch, T. (deposition date: 2021-12-24, release date: 2022-06-08, Last modification date: 2024-07-17)

Primary citation

Pesenti, M.E.,Raisch, T.,Conti, D.,Walstein, K.,Hoffmann, I.,Vogt, D.,Prumbaum, D.,Vetter, I.R.,Raunser, S.,Musacchio, A.
Structure of the human inner kinetochore CCAN complex and its significance for human centromere organization.
Mol.Cell, 82:2113-, 2022

PubMed Abstract: Centromeres are specialized chromosome loci that seed the kinetochore, a large protein complex that effects chromosome segregation. A 16-subunit complex, the constitutive centromere associated network (CCAN), connects between the specialized centromeric chromatin, marked by the histone H3 variant CENP-A, and the spindle-binding moiety of the kinetochore. Here, we report a cryo-electron microscopy structure of human CCAN. We highlight unique features such as the pseudo GTPase CENP-M and report how a crucial CENP-C motif binds the CENP-LN complex. The CCAN structure has implications for the mechanism of specific recognition of the CENP-A nucleosome. A model consistent with our structure depicts the CENP-C-bound nucleosome as connected to the CCAN through extended, flexible regions of CENP-C. An alternative model identifies both CENP-C and CENP-N as specificity determinants but requires CENP-N to bind CENP-A in a mode distinct from the classical nucleosome octamer.

PubMed: 35525244
DOI: 10.1016/j.molcel.2022.04.027

Experimental method

ELECTRON MICROSCOPY (4.6 Å)