6TLX

Crystal structure of the unconventional kinetochore protein Perkinsela sp. KKT2a central domain

Summary for 6TLX

• Entry DOI: 10.2210/pdb6tlx/pdb
• Related: 6TLY
• Descriptor: Protein kinase, ZINC ION (2 entities in total)
• Functional Keywords: kinetochore, zinc finger, kinetoplastid, kkt2, cell cycle
• Biological source: Perkinsela sp. CCAP 1560/4
• Total number of polymer chains: 1
• Total formula weight: 14701.35

Authors

Marciano, G.,Nerusheva, O.,Ishii, M.,Akiyoshi, B. (deposition date: 2019-12-03, release date: 2019-12-25, Last modification date: 2024-05-15)

Primary citation

Marciano, G.,Ishii, M.,Nerusheva, O.O.,Akiyoshi, B.
Kinetoplastid kinetochore proteins KKT2 and KKT3 have unique centromere localization domains.
J.Cell Biol., 220:-, 2021

PubMed Abstract: The kinetochore is the macromolecular protein complex that assembles onto centromeric DNA and binds spindle microtubules. Evolutionarily divergent kinetoplastids have an unconventional set of kinetochore proteins. It remains unknown how kinetochores assemble at centromeres in these organisms. Here, we characterize KKT2 and KKT3 in the kinetoplastid parasite Trypanosoma brucei. In addition to the N-terminal kinase domain and C-terminal divergent polo boxes, these proteins have a central domain of unknown function. We show that KKT2 and KKT3 are important for the localization of several kinetochore proteins and that their central domains are sufficient for centromere localization. Crystal structures of the KKT2 central domain from two divergent kinetoplastids reveal a unique zinc-binding domain (termed the CL domain for centromere localization), which promotes its kinetochore localization in T. brucei. Mutations in the equivalent domain in KKT3 abolish its kinetochore localization and function. Our work shows that the unique central domains play a critical role in mediating the centromere localization of KKT2 and KKT3.

PubMed: 34081090
DOI: 10.1083/jcb.202101022

Experimental method

X-RAY DIFFRACTION (2.87 Å)