› 2lh0

Solution NMR

NMR structure of the histone-interacting N-terminal homodimeric region of Rtt106

Released:
DOI: 10.2210/pdb2lh0/pdb
PDB entry 2lh0 coloured by chain, ensemble of 20 models, front view.
PDB entry 2lh0 coloured by chain, ensemble of 20 models, side view.
PDB entry 2lh0 coloured by chain, ensemble of 20 models, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106.
Su D, Hu Q, Li Q, Thompson JR, Cui G, Fazly A, Davies BA, Botuyan MV, Zhang Z, Mer G
Nature 483 104-7 (2012)
PMID: 22307274

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154040 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone chaperone RTT106 Chains: A, B
Molecule details ›
Chains: A, B
Length: 70 amino acids
Theoretical weight: 8.13 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P40161 (Residues: 1-67; Coverage: 15%)
Gene names: N1346, RTT106, YNL206C
Sequence domains: Histone chaperone Rtt106 N-terminal domain
Structure domains: RTT106-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 46%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

29 review citations

Histone exchange, chromatin structure and the regulation of transcription.
Venkatesh et al. (2015)
28 more

1 mention without citation

Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106.
Su et al. (2012)