4b0t

X-ray diffraction
2.16Å resolution

Structure of the Pup Ligase PafA of the Prokaryotic Ubiquitin-like Modification Pathway in Complex with ADP

Released:
Source organism: Corynebacterium glutamicum
Entry authors: Ozcelik D, Barandun J, Schmitz N, Sutter M, Guth E, Damberger FF, Allain FH-T, Ban N, Weber-Ban E

Function and Biology Details

Reaction catalysed:
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N(6)-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pup--protein ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 493 amino acids
Theoretical weight: 55.23 KDa
Source organism: Corynebacterium glutamicum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8NQE1 (Residues: 1-482; Coverage: 100%)
Gene names: Cgl1494, cg1688, pafA
Sequence domains: Pup-ligase protein

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 62.1Å b: 118.81Å c: 163.02Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.177 0.219
Expression system: Escherichia coli BL21(DE3)