› 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 entry 3tvv coloured by chain, front view.
PDB entry 3tvv coloured by chain, side view.
PDB entry 3tvv coloured by chain, 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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154039 (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

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)