Drosophila melanogaster CENP-C cupin domain

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

TPLRDEQEEASTKLMQWLRGVGDAPPSASMSDENASVSSANELIFCQVDGIDYAFYNTKEKAMLGYMRFKPYQKRSMKQA
KVHPLKLLVQFGEFNVETLAVGEEKEVHSVLRVGDMIEIDRGTRYSIQNAIDKVSVLMCIRS

Purified native D. Melanogaster CENPC 1244 to 1411 protein was mixed with 0.2 M NaCl, 0.1 M MES (pH 6.0), 15 % v/v Pentaerythritol propoxylate (5/4 PO/OH) in a 1:1 ratio (v/v). SeMet substituted crystals were grown in the same condition by providing native crystals as microseeds

D. melanogaster CENP-C 1190-1411 crystals were grown by mixing purified proteins 0.1 M MOPS (pH 7.0) and 12% (w/v) PEG 4000 in a 1:1 ratio (v/v)

National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)

National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)

The construct used for crystallization was D. melanogaster CENP-C 1190-1411 with an additional Ser-Asn-Ala sequence at the N-terminus from the expression tag. Tag and residues 1190-1269 were likely proteolytically cleaved during crystallization and are not visible in the structure.

Cupin, Kinetochore, CENP-C, Drosophila, dimer, CELL CYCLE