› 1euv

X-ray diffraction
1.6Å resolution

X-RAY STRUCTURE OF THE C-TERMINAL ULP1 PROTEASE DOMAIN IN COMPLEX WITH SMT3, THE YEAST ORTHOLOG OF SUMO.

Released:
DOI: 10.2210/pdb1euv/pdb
PDB entry 1euv coloured by chain, front view.
PDB entry 1euv coloured by chain, side view.
PDB entry 1euv coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast.
Mossessova E, Lima CD
Mol Cell 5 865-76 (2000)
PMID: 10882122

Function and Biology Details

Reaction catalysed: 
Hydrolysis of the alpha-linked peptide bond in the sequence Gly-Gly-|-Ala-Thr-Tyr at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptide, Smt3, leading to the mature form of the protein. A second reaction involves the cleavage of an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169741 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin-like-specific protease 1 Chain: A
Molecule details ›
Chain: A
Length: 221 amino acids
Theoretical weight: 25.65 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q02724 (Residues: 403-621; Coverage: 35%)
Gene names: LPB11C, ULP1, YPL020C
Sequence domains: Ulp1 protease family, C-terminal catalytic domain
Structure domains:
Ubiquitin-like protein SMT3 Chain: B
Molecule details ›
Chain: B
Length: 86 amino acids
Theoretical weight: 9.96 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12306 (Residues: 13-98; Coverage: 85%)
Gene names: D9719.15, SMT3, YDR510W
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P21212
Unit cell:
a: 125.774Å b: 53.167Å c: 54.262Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.19 0.251
Expression system: Escherichia coli

Quick links

Citations

46 review citations

Mechanisms underlying ubiquitination.
Pickart CM. (2001)
45 more

30 mentions without citation

Chemoenzymatic Semisynthesis of Proteins.
Thompson et al. (2020)
29 more