4X23: CRYSTAL STRUCTURE OF CENP-C IN COMPLEX WITH THE NUCLEOSOME CORE PARTICLE

Citation:
Abstract
Chromosome segregation during mitosis requires assembly of the kinetochore complex at the centromere. Kinetochore assembly depends on specific recognition of the histone variant CENP-A in the centromeric nucleosome by centromere protein C (CENP-C). We have defined the determinants of this recognition mechanism and discovered that CENP-C binds a hydrophobic region in the CENP-A tail and docks onto the acidic patch of histone H2A and H2B. We further found that the more broadly conserved CENP-C motif uses the same mechanism for CENP-A nucleosome recognition. Our findings reveal a conserved mechanism for protein recruitment to centromeres and a histone recognition mode whereby a disordered peptide binds the histone tail through hydrophobic interactions facilitated by nucleosome docking.
PDB ID: 4X23Download
MMDB ID: 125530
PDB Deposition Date: 2014/11/25
Updated in MMDB: 2017/12
Experimental Method:
x-ray diffraction
Resolution: 3.5  Å
Source Organism:
Homo sapiens
Similar Structures:
Biological Unit for 4X23: tetradecameric; determined by author
Molecular Components in 4X23
Label Count Molecule
Proteins (12 molecules)
2
Histone H3(Gene symbol: His3:CG31613)
Molecule annotation
2
Histone H4(Gene symbol: His4r)
Molecule annotation
2
Histone H2A(Gene symbol: His2A:CG31618)
Molecule annotation
2
Histone H2B(Gene symbol: His2B:CG17949)
Molecule annotation
4
Cenp-c
Molecule annotation
Nucleotides(2 molecules)
1
DNA (147-mer)
Molecule annotation
1
DNA (147-mer)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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