› 4bvu

X-ray diffraction
2.7Å resolution

Structure of Shigella effector OspG in complex with host UbcH5c- Ubiquitin conjugate

Released:
DOI: 10.2210/pdb4bvu/pdb
PDB entry 4bvu coloured by chain, front view.
PDB entry 4bvu coloured by chain, side view.
PDB entry 4bvu coloured by chain, top view.
Source organisms:
Primary publication:
E2~Ub conjugates regulate the kinase activity of Shigella effector OspG during pathogenesis.
Pruneda JN, Smith FD, Daurie A, Swaney DL, Villén J, Scott JD, Stadnyk AW, Le Trong I, Stenkamp RE, Klevit RE, Rohde JR, Brzovic PS
EMBO J 33 437-49 (2014)
PMID: 24446487

Function and Biology Details

Reactions catalysed: 
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
(1a) S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [(E3-independent) E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-monoubiquitinyl-[(E3-independent) ubiquitin-conjugating enzyme]-L-cysteine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-143361 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Protein kinase OspG Chain: A
Molecule details ›
Chain: A
Length: 211 amino acids
Theoretical weight: 24.39 KDa
Source organism: Shigella flexneri
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q99PZ6 (Residues: 1-196; Coverage: 100%)
Gene names: CP0227, SFLP087, ospG, pWR501_0237
Structure domains:
Ubiquitin-conjugating enzyme E2 D3 Chain: B
Molecule details ›
Chain: B
Length: 147 amino acids
Theoretical weight: 16.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P61077 (Residues: 1-147; Coverage: 100%)
Gene names: UBC5C, UBCH5C, UBE2D3
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme
Ubiquitin Chain: C
Molecule details ›
Chain: C
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0CG48 (Residues: 609-684; Coverage: 11%)
Gene name: UBC
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: SSRL BEAMLINE BL9-2
Spacegroup: P6322
Unit cell:
a: 183.873Å b: 183.873Å c: 63.973Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.247 0.244 0.291
Expression system: Escherichia coli BL21

Quick links

Citations

29 review citations

E2 enzymes: more than just middle men.
Stewart et al. (2016)
28 more

7 mentions without citation

Bacterial effectors and their functions in the ubiquitin-proteasome system: insight from the modes of substrate recognition.
Kim et al. (2014)
6 more