› 4p32

X-ray diffraction
1.55Å resolution

Crystal structure of E. coli LptB in complex with ADP-magnesium

Released:
DOI: 10.2210/pdb4p32/pdb
PDB entry 4p32 coloured by chain, front view.
PDB entry 4p32 coloured by chain, side view.
PDB entry 4p32 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Decoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transport.
Sherman DJ, Lazarus MB, Murphy L, Liu C, Walker S, Ruiz N, Kahne D
Proc Natl Acad Sci U S A 111 4982-7 (2014)
PMID: 24639492

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141929 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipopolysaccharide export system ATP-binding protein LptB Chains: A, B
Molecule details ›
Chains: A, B
Length: 249 amino acids
Theoretical weight: 27.94 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A9V1 (Residues: 2-241; Coverage: 100%)
Gene names: JW3168, b3201, lptB, yhbG
Sequence domains:
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
Ligand ADP 2 x ADP
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2
Unit cell:
a: 191.9Å b: 36.02Å c: 64.51Å
α: 90° β: 96.16° γ: 90°
R-values:
R R work R free
0.199 0.198 0.218
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

15 review citations

Function and Biogenesis of Lipopolysaccharides.
Bertani et al. (2018)
14 more

3 mentions without citation

Lipopolysaccharide transport to the cell surface: biosynthesis and extraction from the inner membrane.
Simpson et al. (2015)
2 more