› 2ly8

Solution NMR

The budding yeast chaperone Scm3 recognizes the partially unfolded dimer of the centromere-specific Cse4/H4 histone variant

Released:
DOI: 10.2210/pdb2ly8/pdb
PDB entry 2ly8 coloured by chain, ensemble of 10 models, front view.
PDB entry 2ly8 coloured by chain, ensemble of 10 models, side view.
PDB entry 2ly8 coloured by chain, ensemble of 10 models, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Identification of functionally conserved regions in the structure of the chaperone/CenH3/H4 complex.
Hong J, Feng H, Zhou Z, Ghirlando R, Bai Y
J Mol Biol 425 536-45 (2013)
PMID: 23178171

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153100 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone H3-like centromeric protein CSE4 Chain: A
Molecule details ›
Chain: A
Length: 121 amino acids
Theoretical weight: 13.72 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P36012 (Residues: 152-207, 208-212; Coverage: 27%)
Gene names: CSE4, CSL2, YKL049C, YKL262
Sequence domains: Core histone H2A/H2B/H3/H4
Structure domains: Histone, subunit A

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 88%
Refinement method: DGSA-distance geometry simulated annealing
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

A network of players in H3 histone variant deposition and maintenance at centromeres.
Müller et al. (2014)
6 other articles