7X85

Crystal structure of chicken CENP-C Cupin domain

Summary for 7X85

• Entry DOI: 10.2210/pdb7x85/pdb
• Descriptor: CENP-C, CITRIC ACID, GLYCEROL, ... (4 entities in total)
• Functional Keywords: kinetochore, centromere, chromosome segregation, dimerization, cell cycle
• Biological source: Gallus gallus (chicken)
• Total number of polymer chains: 3
• Total formula weight: 64664.78

Authors

Ariyoshi, M.,Hara, M.,Fukagawa, T. (deposition date: 2022-03-11, release date: 2023-03-15, Last modification date: 2023-11-29)

Primary citation

Hara, M.,Ariyoshi, M.,Sano, T.,Nozawa, R.S.,Shinkai, S.,Onami, S.,Jansen, I.,Hirota, T.,Fukagawa, T.
Centromere/kinetochore is assembled through CENP-C oligomerization.
Mol.Cell, 83:2188-2205.e13, 2023

PubMed Abstract: Kinetochore is an essential protein complex required for accurate chromosome segregation. The constitutive centromere-associated network (CCAN), a subcomplex of the kinetochore, associates with centromeric chromatin and provides a platform for the kinetochore assembly. The CCAN protein CENP-C is thought to be a central hub for the centromere/kinetochore organization. However, the role of CENP-C in CCAN assembly needs to be elucidated. Here, we demonstrate that both the CCAN-binding domain and the C-terminal region that includes the Cupin domain of CENP-C are necessary and sufficient for chicken CENP-C function. Structural and biochemical analyses reveal self-oligomerization of the Cupin domains of chicken and human CENP-C. We find that the CENP-C Cupin domain oligomerization is vital for CENP-C function, centromeric localization of CCAN, and centromeric chromatin organization. These results suggest that CENP-C facilitates the centromere/kinetochore assembly through its oligomerization.

PubMed: 37295434
DOI: 10.1016/j.molcel.2023.05.023

Experimental method

X-RAY DIFFRACTION (2.639 Å)