6O2K

Drosophila melanogaster CENP-C cupin domain

6O2K の概要

• エントリーDOI: 10.2210/pdb6o2k/pdb
• 分子名称: Centromeric protein-C, isoform A (2 entities in total)
• 機能のキーワード: cupin, kinetochore, cenp-c, drosophila, dimer, cell cycle
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32146.77

構造登録者

Chik, J.K.,Cho, U.S. (登録日: 2019-02-23, 公開日: 2019-08-21, 最終更新日: 2024-03-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.81 Å)