› 3to1

X-ray diffraction
2.6Å resolution

Two surfaces on Rtt106 mediate histone binding and chaperone activity

Released:
DOI: 10.2210/pdb3to1/pdb
PDB entry 3to1 coloured by chain, front view.
PDB entry 3to1 coloured by chain, side view.
PDB entry 3to1 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Two surfaces on the histone chaperone Rtt106 mediate histone binding, replication, and silencing.
Zunder RM, Antczak AJ, Berger JM, Rine J
Proc Natl Acad Sci U S A 109 E144-53 (2012)
PMID: 22198837

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: 235 amino acids
Theoretical weight: 26.89 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P40161 (Residues: 69-300; Coverage: 51%)
Gene names: N1346, RTT106, YNL206C
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21
Unit cell:
a: 71.977Å b: 60.703Å c: 76.411Å
α: 90° β: 104.52° γ: 90°
R-values:
R R work R free
0.212 0.21 0.257
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Histone core modifications regulating nucleosome structure and dynamics.
Tessarz et al. (2014)
6 more

1 mention without citation

Two surfaces on the histone chaperone Rtt106 mediate histone binding, replication, and silencing.
Zunder et al. (2012)