› 5v1a

X-ray diffraction
2.14Å resolution

Structure of S. cerevisiae Ulp2:Csm1 complex

Released:
DOI: 10.2210/pdb5v1a/pdb
PDB entry 5v1a coloured by chain, front view.
PDB entry 5v1a coloured by chain, side view.
PDB entry 5v1a coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Recruitment of a SUMO isopeptidase to rDNA stabilizes silencing complexes by opposing SUMO targeted ubiquitin ligase activity.
Liang J, Singh N, Carlson CR, Albuquerque CP, Corbett KD, Zhou H
Genes Dev 31 802-815 (2017)
PMID: 28487408

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150540 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin-like-specific protease 2 Chain: B
Molecule details ›
Chain: B
Length: 26 amino acids
Theoretical weight: 2.89 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P40537 (Residues: 821-845; Coverage: 2%)
Gene names: SMT4, ULP2, YIL031W
Monopolin complex subunit CSM1 Chain: A
Molecule details ›
Chain: A
Length: 122 amino acids
Theoretical weight: 14.14 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P25651 (Residues: 69-190; Coverage: 64%)
Gene names: CSM1, SPO86, YCR086W, YCR86W
Sequence domains: Chromosome segregation protein Csm1/Pcs1
Structure domains: Aspartate Aminotransferase, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL14-1
Spacegroup: P43212
Unit cell:
a: 46.737Å b: 46.737Å c: 124.638Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.234 0.278
Expression system: Escherichia coli

Quick links

Citations

5 review citations

SUMO-Mediated Regulation of Nuclear Functions and Signaling Processes.
Zhao X. (2018)
4 more