6ZPK
Crystal structure of the unconventional kinetochore protein Trypanosoma brucei KKT4 BRCT domain
Summary for 6ZPK
| Entry DOI | 10.2210/pdb6zpk/pdb |
| Descriptor | Trypanosoma brucei KKT4 463-645, GLYCEROL, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | kinetochore, kinetoplastid, kkt4, brct, cell cycle |
| Biological source | Trypanosoma brucei brucei (strain 927/4 GUTat10.1) |
| Total number of polymer chains | 1 |
| Total formula weight | 20319.13 |
| Authors | Ludzia, P.,Lowe, E.D.,Marciano, G.,Mohammed, S.,Redfield, C.,Akiyoshi, B. (deposition date: 2020-07-08, release date: 2020-10-21, Last modification date: 2024-06-19) |
| Primary citation | Ludzia, P.,Lowe, E.D.,Marciano, G.,Mohammed, S.,Redfield, C.,Akiyoshi, B. Structural characterization of KKT4, an unconventional microtubule-binding kinetochore protein. Structure, 29:1014-1028.e8, 2021 Cited by PubMed Abstract: The kinetochore is the macromolecular machinery that drives chromosome segregation by interacting with spindle microtubules. Kinetoplastids (such as Trypanosoma brucei), a group of evolutionarily divergent eukaryotes, have a unique set of kinetochore proteins that lack any significant homology to canonical kinetochore components. To date, KKT4 is the only kinetoplastid kinetochore protein that is known to bind microtubules. Here we use X-ray crystallography, NMR spectroscopy, and crosslinking mass spectrometry to characterize the structure and dynamics of KKT4. We show that its microtubule-binding domain consists of a coiled-coil structure followed by a positively charged disordered tail. The structure of the C-terminal BRCT domain of KKT4 reveals that it is likely a phosphorylation-dependent protein-protein interaction domain. The BRCT domain interacts with the N-terminal region of the KKT4 microtubule-binding domain and with a phosphopeptide derived from KKT8. Taken together, these results provide structural insights into the unconventional kinetoplastid kinetochore protein KKT4. PubMed: 33915106DOI: 10.1016/j.str.2021.04.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.57 Å) |
Structure validation
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