› 4b0s

X-ray diffraction
2.85Å resolution

Structure of the Deamidase-Depupylase Dop of the Prokaryotic Ubiquitin-like Modification Pathway in Complex with ATP

Released:
DOI: 10.2210/pdb4b0s/pdb
PDB entry 4b0s coloured by chain, front view.
PDB entry 4b0s coloured by chain, side view.
PDB entry 4b0s coloured by chain, top view.
Source organism: Acidothermus cellulolyticus 11B
Primary publication:
Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathway.
Özcelik D, Barandun J, Schmitz N, Sutter M, Guth E, Damberger FF, Allain FH, Ban N, Weber-Ban E
Nat Commun 3 1014 (2012)
PMID: 22910360

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106122 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Depupylase Chain: A
Molecule details ›
Chain: A
Length: 506 amino acids
Theoretical weight: 57.13 KDa
Source organism: Acidothermus cellulolyticus 11B
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0LU48 (Residues: 1-501; Coverage: 100%)
Gene names: Acel_1186, dop
Sequence domains: Pup-ligase protein

Ligands and Environments

2 bound ligands:
Ligand ATP 1 x ATP
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 65.36Å b: 70.41Å c: 93.52Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.189 0.246
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Pupylation as a signal for proteasomal degradation in bacteria.
Striebel et al. (2014)
8 more

3 mentions without citation

Prokaryotic ubiquitin-like protein modification.
Maupin-Furlow JA. (2014)
2 more