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PDBsum entry 2fv4
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Structural protein, protein binding
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PDB id
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2fv4
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References listed in PDB file
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Key reference
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Title
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Structure of a central component of the yeast kinetochore: the spc24p/spc25p globular domain.
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Authors
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R.R.Wei,
J.R.Schnell,
N.A.Larsen,
P.K.Sorger,
J.J.Chou,
S.C.Harrison.
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Ref.
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Structure, 2006,
14,
1003-1009.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 1.
Figure 1. Schematic Diagram of the Ndc80 Complex
MT,
microtubule; CEN, centromere. Each subunit is represented by an
oval (the globular domain) and a stick (the coiled-coil region).
The coiled-coils of Ndc80p/Nuf2p and Spc24p/Spc25p form the
shaft. The globular domains of Ndc80p/Nuf2p form the “outer”
head, which faces the microtubule; the globular domains of the
Spc24p/Spc25p, the “inner” head, which faces the centromere.
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Figure 2.
Figure 2. Overview of the NMR and Crystal Structures of
Spc24G/Spc25G
(A) Superposition of the backbones of the
solution NMR structure (light blue) and crystal structure
(gold). The dotted lines represent unstructured residues
138–154 of Spc24G and 128–132 of Spc25G. The N and C termini
of Spc24G and Spc25G are labeled with “ 24N,” “24C,”
“25N,” and “25C,” respectively.
(B) Ribbon diagram
of the crystal structure in the same view as in (A). The α
helices and β strands are orange and yellow in Spc24G and green
and blue in Spc25G, respectively.
(C) Folding diagram of
Spc24G and Spc25G. The secondary structures are colored as in
(B). The N and C termini are labeled with “N” and “C,”
respectively.
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The above figures are
reprinted
by permission from Cell Press:
Structure
(2006,
14,
1003-1009)
copyright 2006.
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