› 1oxx

X-ray diffraction
1.45Å resolution

Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus

Released:
DOI: 10.2210/pdb1oxx/pdb
Model geometry
Fit model/data
PDB entry 1oxx coloured by chain, front view.
PDB entry 1oxx coloured by chain, side view.
PDB entry 1oxx coloured by chain, top view.
Source organism: Saccharolobus solfataricus
Primary publication:
Formation of the productive ATP-Mg2+-bound dimer of GlcV, an ABC-ATPase from Sulfolobus solfataricus.
Verdon G, Albers SV, van Oosterwijk N, Dijkstra BW, Driessen AJ, Thunnissen AM
J Mol Biol 334 255-67 (2003)
PMID: 14607117

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188982 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose import ATP-binding protein GlcV Chain: K
Molecule details ›
Chain: K
Length: 353 amino acids
Theoretical weight: 39.18 KDa
Source organism: Saccharolobus solfataricus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q97UY8 (Residues: 1-353; Coverage: 100%)
Gene names: SSO2850, glcV
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand IOD 32 x IOD
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 46.282Å b: 48.427Å c: 183.533Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.172 0.213
Expression system: Escherichia coli

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Citations

15 review citations

Structure, function, and evolution of bacterial ATP-binding cassette systems.
Davidson et al. (2008)
14 more

4 mentions without citation

Decoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transport.
Sherman et al. (2014)
3 more