› 5c78

X-ray diffraction
2.9Å resolution

ATP-driven lipid-linked oligosaccharide flippase PglK in apo-inward state (1)

Released:
DOI: 10.2210/pdb5c78/pdb
PDB entry 5c78 coloured by chain, front view.
PDB entry 5c78 coloured by chain, side view.
PDB entry 5c78 coloured by chain, top view.
Source organism: Campylobacter jejuni
Primary publication:
Structure and mechanism of an active lipid-linked oligosaccharide flippase.
Perez C, Gerber S, Boilevin J, Bucher M, Darbre T, Aebi M, Reymond JL, Locher KP
Nature 524 433-8 (2015)
PMID: 26266984

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131458 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
WlaB protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 564 amino acids
Theoretical weight: 64.59 KDa
Source organism: Campylobacter jejuni
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O86150 (Residues: 1-564; Coverage: 100%)
Gene names: JYC20_000392, pglK, wlaB
Sequence domains:
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

1 bound ligand:
Ligand 1PE 5 x 1PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P1
Unit cell:
a: 96.6Å b: 114.42Å c: 145.59Å
α: 68.44° β: 73.27° γ: 68.67°
R-values:
R R work R free
0.233 0.232 0.267
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

29 review citations

Mechanistic diversity in ATP-binding cassette (ABC) transporters.
Locher KP. (2016)
28 more

2 mentions without citation

Structural and functional diversity calls for a new classification of ABC transporters.
Thomas et al. (2020)
1 more