NMR study of the structure and dynamics of the BRCT domain from the kinetochore protein KKT4.

ABSTRACT: KKT4 is a multi-domain kinetochore protein specific to kinetoplastids, such as Trypanosoma brucei. It lacks significant sequence similarity to known kinetochore proteins in other eukaryotes. Our recent X-ray structure of the C-terminal region of KKT4 shows that it has a tandem BRCT (BRCA1 C Terminus) domain fold with a sulfate ion bound in a typical binding site for a phosphorylated serine or threonine. Here we present the ¹H, ¹³C and ¹⁵N resonance assignments for the BRCT domain of KKT4 (KKT4^463-645) from T. brucei. We show that the BRCT domain can bind phosphate ions in solution using residues involved in sulfate ion binding in the X-ray structure. We have used these assignments to characterise the secondary structure and backbone dynamics of t

SUBMITTER: Ludzia P 

PROVIDER: S-EPMC11081923 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature