6O2D

Schizosaccharomyces pombe Cnp3 Cupin Domain

Summary for 6O2D

• Entry DOI: 10.2210/pdb6o2d/pdb
• Descriptor: Inner kinetochore subunit cnp3 (2 entities in total)
• Functional Keywords: cenp-c, kinetochore, cupin, dimer, cell cycle
• Biological source: Schizosaccharomyces pombe (Fission yeast)
• Total number of polymer chains: 2
• Total formula weight: 36097.67

Authors

Chik, J.K.,Cho, U.S. (deposition date: 2019-02-22, release date: 2019-08-21, Last modification date: 2024-10-23)

Primary citation

Chik, J.K.,Moiseeva, V.,Goel, P.K.,Meinen, B.A.,Koldewey, P.,An, S.,Mellone, B.G.,Subramanian, L.,Cho, U.S.
Structures of CENP-C cupin domains at regional centromeres reveal unique patterns of dimerization and recruitment functions for the inner pocket.
J.Biol.Chem., 294:14119-14134, 2019

PubMed Abstract: The successful assembly and regulation of the kinetochore are critical for the equal and accurate segregation of genetic material during the cell cycle. CENP-C (centromere protein C), a conserved inner kinetochore component, has been broadly characterized as a scaffolding protein and is required for the recruitment of multiple kinetochore proteins to the centromere. At its C terminus, CENP-C harbors a conserved cupin domain that has an established role in protein dimerization. Although the crystal structure of the Mif2 cupin domain has been determined, centromeric organization and kinetochore composition vary greatly between (point centromere) and other eukaryotes (regional centromere). Therefore, whether the structural and functional role of the cupin domain is conserved throughout evolution requires investigation. Here, we report the crystal structures of the and CENP-C cupin domains at 2.52 and 1.81 Å resolutions, respectively. Although the central jelly roll architecture is conserved among the three determined CENP-C cupin domain structures, the cupin domains from organisms with regional centromeres contain additional structural features that aid in dimerization. Moreover, we found that the Cnp3 jelly roll fold harbors an inner binding pocket that is used to recruit the meiosis-specific protein Moa1. In summary, our results unveil the evolutionarily conserved and unique features of the CENP-C cupin domain and uncover the mechanism by which it functions as a recruitment factor.

PubMed: 31366733
DOI: 10.1074/jbc.RA119.008464

Experimental method

X-RAY DIFFRACTION (2.52 Å)