3SQI
DNA binding domain of Ndc10
Summary for 3SQI
Entry DOI | 10.2210/pdb3sqi/pdb |
Descriptor | KLLA0E03807p, DNA (5'-D(P*TP*TP*AP*AP*TP*TP*TP*AP*TP*AP*AP*AP*AP*TP*T)-3'), DNA (5'-D(P*AP*AP*AP*TP*TP*TP*TP*AP*TP*AP*AP*AP*TP*TP*A)-3') (3 entities in total) |
Functional Keywords | dna recombinase, dna binding, dna, dna binding protein-dna complex, dna binding protein/dna |
Biological source | Kluyveromyces lactis (yeast) More |
Total number of polymer chains | 3 |
Total formula weight | 70681.95 |
Authors | Cho, U.S.,Harrison, S.C. (deposition date: 2011-07-05, release date: 2011-12-07, Last modification date: 2024-02-28) |
Primary citation | Cho, U.S.,Harrison, S.C. Ndc10 is a platform for inner kinetochore assembly in budding yeast. Nat.Struct.Mol.Biol., 19:48-55, 2011 Cited by PubMed Abstract: Kinetochores link centromeric DNA to spindle microtubules and ensure faithful chromosome segregation during mitosis. In point-centromere yeasts, the CBF3 complex Skp1-Ctf13-(Cep3)(2)-(Ndc10)(2) recognizes a conserved centromeric DNA element through contacts made by Cep3 and Ndc10. We describe here the five-domain organization of Kluyveromyces lactis Ndc10 and the structure at 2.8 Å resolution of domains I-II (residues 1-402) bound to DNA. The structure resembles tyrosine DNA recombinases, although it lacks both endonuclease and ligase activities. Structural and biochemical data demonstrate that each subunit of the Ndc10 dimer binds a separate fragment of DNA, suggesting that Ndc10 stabilizes a DNA loop at the centromere. We describe in vitro association experiments showing that specific domains of Ndc10 interact with each of the known inner-kinetochore proteins or protein complexes in budding yeast. We propose that Ndc10 provides a central platform for inner-kinetochore assembly. PubMed: 22139014DOI: 10.1038/nsmb.2178 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8245 Å) |
Structure validation
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