9EVQ
Crystal structure of the kinetoplastid kinetochore protein KKT23 acetyltransferase domain from Trypanosoma brucei
Summary for 9EVQ
| Entry DOI | 10.2210/pdb9evq/pdb |
| Descriptor | N-acetyltransferase domain-containing protein, ACETYL COENZYME *A (3 entities in total) |
| Functional Keywords | kinetochore, kinetoplastid, histone, acetyltransferase, mitosis, cell cycle |
| Biological source | Trypanosoma brucei brucei TREU927 |
| Total number of polymer chains | 2 |
| Total formula weight | 53861.26 |
| Authors | Ludzia, P.,Ishii, M.,Akiyoshi, B. (deposition date: 2024-04-01, release date: 2024-08-28, Last modification date: 2025-01-15) |
| Primary citation | Ludzia, P.,Ishii, M.,Deak, G.,Spanos, C.,Wilson, M.D.,Redfield, C.,Akiyoshi, B. The kinetoplastid kinetochore protein KKT23 acetyltransferase is a structural homolog of GCN5 that acetylates the histone H2A C-terminal tail. Structure, 33:123-, 2025 Cited by PubMed Abstract: The kinetochore is the macromolecular protein machine that drives chromosome segregation in eukaryotes. In an evolutionarily divergent group of organisms called kinetoplastids, kinetochores are built using a unique set of proteins (KKT1-25 and KKIP1-12). KKT23 is a constitutively localized kinetochore protein containing a C-terminal acetyltransferase domain of unknown function. Here, using X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy, we have determined the structure and dynamics of the KKT23 acetyltransferase domain from Trypanosoma brucei and found that it is structurally similar to the GCN5 histone acetyltransferase domain. We find that KKT23 can acetylate the C-terminal tail of histone H2A and that knockdown of KKT23 results in decreased H2A acetylation levels in T. brucei. Finally, we have determined the crystal structure of the N-terminal region of KKT23 and shown that it interacts with KKT22. Our study provides important insights into the structure and function of the unique kinetochore acetyltransferase in trypanosomes. PubMed: 39579771DOI: 10.1016/j.str.2024.10.031 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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