6P7X

Structure of the K. lactis CBF3 core - Ndc10 D1D2 complex

Summary for 6P7X

• Entry DOI: 10.2210/pdb6p7x/pdb
• EMDB information: 20270 20271 20272
• Descriptor: Ndc10, Ctf13, Skp1, ... (4 entities in total)
• Functional Keywords: yeast centromere-binding complex, dna binding protein
• Biological source: Kluyveromyces lactis (Yeast); More
• Total number of polymer chains: 5
• Total formula weight: 262625.43

Authors

Lee, P.D.,Wei, H.,Tan, D.,Harrison, S.C. (deposition date: 2019-06-06, release date: 2019-09-18, Last modification date: 2024-03-20)

Primary citation

Lee, P.D.,Wei, H.,Tan, D.,Harrison, S.C.
Structure of the Centromere Binding Factor 3 Complex from Kluyveromyces lactis.
J.Mol.Biol., 431:4444-4454, 2019

PubMed Abstract: Kinetochores are the multiprotein complexes that link chromosomal centromeres to mitotic-spindle microtubules. Budding yeast centromeres comprise three sequential "centromere-determining elements", CDEI, II, and III. CDEI (8 bp) and CDEIII (∼25 bp) are conserved between Kluyveromyces lactis and Saccharomyces cerevisiae, but CDEII in the former is twice as long (160 bp) as CDEII in the latter (80 bp). The CBF3 complex recognizes CDEIII and is required for assembly of a centromeric nucleosome, which in turn recruits other kinetochore components. To understand differences in centromeric nucleosome assembly between K. lactis and S. cerevisiae, we determined the structure of a K. lactis CBF3 complex by electron cryomicroscopy at ∼4 Å resolution and compared it with published structures of S. cerevisiae CBF3. We show differences in the pose of Ndc10 and discuss potential models of the K. lactis centromeric nucleosome that account for the extended CDEII length.

PubMed: 31425683
DOI: 10.1016/j.jmb.2019.08.003

Experimental method

ELECTRON MICROSCOPY (4.3 Å)