PDBsum entry 6o2d

Cell cycle

PDB id: 6o2d

Contents

Protein chains

137 a.a.

145 a.a.

Waters ×5

PDB id:

6o2d

Name:

Cell cycle

Title:

Schizosaccharomyces pombe cnp3 cupin domain

Structure:

Inner kinetochore subunit cnp3. Chain: a, b. Fragment: cupin domain. Synonym: cenp-c homolog,centromere protein 3,constitutive centromere- associated network protein cnp3. Engineered: yes

Source:

Schizosaccharomyces pombe. Fission yeast. Organism_taxid: 4896. Gene: cnp3, spbc1861.01c, spbc56f2.13. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.52Å R-factor: 0.219 R-free: 0.251

Authors:

J.K.Chik,U.S.Cho

Key ref:

J.K.Chik et al. (2019). 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. PubMed id: 31366733 DOI: 10.1074/jbc.RA119.008464

Date:

22-Feb-19 Release date: 21-Aug-19

Protein chain

Q9USR9  (CENPC_SCHPO) -  Inner kinetochore subunit cnp3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843)

Seq: 643 a.a.

Struc: 137 a.a.

Protein chain

Q9USR9  (CENPC_SCHPO) -  Inner kinetochore subunit cnp3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843)

Seq: 643 a.a.

Struc: 145 a.a.

DOI no: 10.1074/jbc.RA119.008464

J Biol Chem 294:14119-14134 (2019)

PubMed id: 31366733

Structures of CENP-C cupin domains at regional centromeres reveal unique patterns of dimerization and recruitment functions for the inner pocket.

J.K.Chik, V.Moiseeva, P.K.Goel, B.A.Meinen, P.Koldewey, S.An, B.G.Mellone, L.Subramanian, U.S.Cho.

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 Saccharomyces cerevisiae Mif2^CENP-C cupin domain has been determined, centromeric organization and kinetochore composition vary greatly between S. cerevisiae (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 Schizosaccharomyces pombe and Drosophila melanogaster 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 S. pombe Cnp3^CENP-C 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.