› 3v62

X-ray diffraction
2.9Å resolution

Structure of the S. cerevisiae Srs2 C-terminal domain in complex with PCNA conjugated to SUMO on lysine 164

Released:
DOI: 10.2210/pdb3v62/pdb
PDB entry 3v62 coloured by chain, front view.
PDB entry 3v62 coloured by chain, side view.
PDB entry 3v62 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Recognition of SUMO-modified PCNA requires tandem receptor motifs in Srs2.
Armstrong AA, Mohideen F, Lima CD
Nature 483 59-63 (2012)
PMID: 22382979

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-146398 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ubiquitin-like protein SMT3 Chains: A, D
Molecule details ›
Chains: A, D
Length: 84 amino acids
Theoretical weight: 9.88 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q12306 (Residues: 20-98; Coverage: 78%)
Gene names: D9719.15, SMT3, YDR510W
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Proliferating cell nuclear antigen Chains: B, E
Molecule details ›
Chains: B, E
Length: 258 amino acids
Theoretical weight: 28.87 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P15873 (Residues: 1-258; Coverage: 100%)
Gene names: POL30, YBR0811, YBR088C
Sequence domains:
Structure domains: Proliferating Cell Nuclear Antigen
ATP-dependent DNA helicase SRS2 Chains: C, F
Molecule details ›
Chains: C, F
Length: 69 amino acids
Theoretical weight: 7.7 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P12954 (Residues: 1107-1174; Coverage: 6%)
Gene names: HPR5, J0913, RADH, SRS2, YJL092W

Ligands and Environments

2 bound ligands:
Ligand NEQ 4 x NEQ
Ligand SO4 4 x SO4
1 modified residue:
Ligand MLY 12 x MLY

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2
Unit cell:
a: 196.817Å b: 62.256Å c: 139.247Å
α: 90° β: 135.04° γ: 90°
R-values:
R R work R free
0.187 0.184 0.237
Expression systems:
  • Escherichia coli BL21(DE3)
  • Escherichia coli

Quick links

Citations

34 review citations

Sumoylation: a regulatory protein modification in health and disease.
Flotho et al. (2013)
33 more

6 mentions without citation

Maneuvers on PCNA Rings during DNA Replication and Repair.
Slade D. (2018)
5 more