› 3tvv

X-ray diffraction
2.59Å resolution

Structure of the tandem PH domains of Rtt106 (residues 68-315)

Released:
DOI: 10.2210/pdb3tvv/pdb
PDB 3tvv coloured by chain and viewed from the front.
PDB 3tvv coloured by chain and viewed from the side.
PDB 3tvv coloured by chain and viewed from the top.
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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone chaperone RTT106 Chains: A, B
Molecule details ›
Chains: A, B
Length: 251 amino acids
Theoretical weight: 29.13 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P40161 (Residues: 68-315; Coverage: 55%)
Gene names: N1346, RTT106, YNL206C
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 14 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 70.66Å b: 60.64Å c: 77.17Å
α: 90° β: 102.49° γ: 90°
R-values:
R R work R free
0.241 0.238 0.294
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

25 review citations

Mechanisms of chromatin-based epigenetic inheritance.
Du et al. (2022)
24 more

1 mention without citation

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