› 2fgk

X-ray diffraction
2.7Å resolution

Crystal structure of the ABC-cassette E631Q mutant of HlyB with bound ATP

Released:
DOI: 10.2210/pdb2fgk/pdb
PDB entry 2fgk coloured by chain, front view.
PDB entry 2fgk coloured by chain, side view.
PDB entry 2fgk coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer.
Zaitseva J, Oswald C, Jumpertz T, Jenewein S, Wiedenmann A, Holland IB, Schmitt L
EMBO J 25 3432-43 (2006)
PMID: 16858415

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140359 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-hemolysin translocation ATP-binding protein HlyB Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 247 amino acids
Theoretical weight: 27.75 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P08716 (Residues: 467-707; Coverage: 34%)
Gene name: hlyB
Sequence domains: ABC transporter
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

1 bound ligand:
Ligand ATP 4 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P21
Unit cell:
a: 47.142Å b: 189.256Å c: 63.475Å
α: 90° β: 111.87° γ: 90°
R-values:
R R work R free
0.226 0.223 0.28
Expression system: Escherichia coli

Quick links

Citations

21 review citations

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

5 mentions without citation

A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer.
Zaitseva et al. (2006)
4 more