› 3owt

X-ray diffraction
2Å resolution

Crystal structure of S. cerevisiae RAP1-Sir3 complex

Released:
DOI: 10.2210/pdb3owt/pdb
PDB entry 3owt coloured by chain, front view.
PDB entry 3owt coloured by chain, side view.
PDB entry 3owt coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
A conserved motif within RAP1 has diversified roles in telomere protection and regulation in different organisms.
Chen Y, Rai R, Zhou ZR, Kanoh J, Ribeyre C, Yang Y, Zheng H, Damay P, Wang F, Tsujii H, Hiraoka Y, Shore D, Hu HY, Chang S, Lei M
Nat Struct Mol Biol 18 213-21 (2011)
PMID: 21217703

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139139 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DNA-binding protein RAP1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 157 amino acids
Theoretical weight: 18.22 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P11938 (Residues: 672-827; Coverage: 19%)
Gene names: GRF1, N1310, RAP1, TUF1, YNL216W
Sequence domains: TRF2-interacting telomeric protein/Rap1 - C terminal domain
Structure domains:
Regulatory protein SIR3 Chain: C
Molecule details ›
Chain: C
Length: 27 amino acids
Theoretical weight: 3.15 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P06701 (Residues: 456-481; Coverage: 3%)
Gene names: CMT1, L9753.10, MAR2, SIR3, STE8, YLR442C

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: R32
Unit cell:
a: 89.831Å b: 89.831Å c: 211.791Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.21 0.26
Expression system: Escherichia coli

Quick links

Citations

18 review citations

Shelterin-Mediated Telomere Protection.
de Lange T. (2018)
17 more

3 mentions without citation

Telomerase and telomere-associated proteins: structural insights into mechanism and evolution.
Lewis et al. (2012)
2 more