2FV4

NMR solution structure of the yeast kinetochore Spc24/Spc25 globular domain

Summary for 2FV4

• Entry DOI: 10.2210/pdb2fv4/pdb
• Related: 2FTX
• Descriptor: Hypothetical 25.2 kDa protein in AFG3-SEB2 intergenic region, Hypothetical 24.6 kDa protein in ILV2-ADE17 intergenic region (2 entities in total)
• Functional Keywords: alpha-beta, complex, coiled-coil, structural protein, protein binding
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Nucleus: P40014 Q04477
• Total number of polymer chains: 2
• Total formula weight: 19512.15

Authors

Schnell, J.R.,Chou, J.J. (deposition date: 2006-01-29, release date: 2006-06-13, Last modification date: 2024-05-29)

Primary citation

Wei, R.R.,Schnell, J.R.,Larsen, N.A.,Sorger, P.K.,Chou, J.J.,Harrison, S.C.
Structure of a central component of the yeast kinetochore: the spc24p/spc25p globular domain.
Structure, 6:1003-1009, 2006

PubMed Abstract: The Ndc80 complex, a kinetochore component conserved from yeast to humans, is essential for proper chromosome alignment and segregation during mitosis. It is an approximately 570 A long, rod-shaped assembly of four proteins--Ndc80p (Hec1), Nuf2p, Spc24p, and Spc25p--with globular regions at either end of a central shaft. The complex bridges from the centromere-proximal inner kinetochore layer at its Spc24/Spc25 globular end to the microtubule binding outer kinetochore layer at its Ndc80/Nuf2 globular end. We report the atomic structures of the Spc24/Spc25 globular domain, determined both by X-ray crystallography at 1.9 A resolution and by NMR. Spc24 and Spc25 fold tightly together into a single globular entity with pseudo-2-fold symmetry. Conserved residues line a common hydrophobic core and the bottom of a cleft, indicating that the functional orthologs from other eukaryotes will have the same structure and suggesting a docking site for components of the inner kinetochore.

PubMed: 16765893
DOI: 10.1016/j.str.2006.04.007

Experimental method

SOLUTION NMR