› 1uhm

Solution NMR

Solution structure of the globular domain of linker histone homolog Hho1p from S. cerevisiae

Released:
DOI: 10.2210/pdb1uhm/pdb
PDB entry 1uhm coloured by chain, ensemble of 20 models, front view.
PDB entry 1uhm coloured by chain, ensemble of 20 models, side view.
PDB entry 1uhm coloured by chain, ensemble of 20 models, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
The linker histone homolog Hho1p from Saccharomyces cerevisiae represents a winged helix-turn-helix fold as determined by NMR spectroscopy.
Ono K, Kusano O, Shimotakahara S, Shimizu M, Yamazaki T, Shindo H
Nucleic Acids Res 31 7199-207 (2003)
PMID: 14654695

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156808 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone H1 Chain: A
Molecule details ›
Chain: A
Length: 78 amino acids
Theoretical weight: 8.52 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P53551 (Residues: 41-118; Coverage: 30%)
Gene names: HHO1, LPI17C, YPL127C
Sequence domains: linker histone H1 and H5 family
Structure domains: Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry simulated annealing molecular dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

What functions do linker histones provide?
Harvey et al. (2004)
2 more

1 mention without citation

The linker histone homolog Hho1p from Saccharomyces cerevisiae represents a winged helix-turn-helix fold as determined by NMR spectroscopy.
Ono et al. (2003)