› 5uf5

X-ray diffraction
2.4Å resolution

Structure of the effector protein SidK (lpg0968) from Legionella pneumophila (domain-swapped dimer)

Released:
DOI: 10.2210/pdb5uf5/pdb
PDB entry 5uf5 coloured by chain, front view.
PDB entry 5uf5 coloured by chain, side view.
PDB entry 5uf5 coloured by chain, top view.
Source organism: Legionella pneumophila
Primary publication:
Molecular basis for the binding and modulation of V-ATPase by a bacterial effector protein.
Zhao J, Beyrakhova K, Liu Y, Alvarez CP, Bueler SA, Xu L, Xu C, Boniecki MT, Kanelis V, Luo ZQ, Cygler M, Rubinstein JL
OpenAccess logo PLoS Pathog 13 e1006394 (2017)
PMID: 28570695

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178689 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Type IV secretion protein Dot Chains: A, B
Molecule details ›
Chains: A, B
Length: 266 amino acids
Theoretical weight: 30.64 KDa
Source organism: Legionella pneumophila
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5ZWW6 (Residues: 16-278; Coverage: 46%)
Gene name: lpg0968

Ligands and Environments

1 bound ligand:
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: C2
Unit cell:
a: 162.08Å b: 41.14Å c: 94.15Å
α: 90° β: 108.39° γ: 90°
R-values:
R R work R free
0.197 0.195 0.23
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Regulation of V-ATPase Activity and Organelle pH by Phosphatidylinositol Phosphate Lipids.
Banerjee et al. (2020)
8 more

1 mention without citation

Molecular basis for the binding and modulation of V-ATPase by a bacterial effector protein.
Zhao et al. (2017)