› 4b54

X-ray diffraction
2.8Å resolution

The Structure of the inactive mutant G153R of LptC from E. coli

Released:
DOI: 10.2210/pdb4b54/pdb
PDB entry 4b54 coloured by chain, front view.
PDB entry 4b54 coloured by chain, side view.
PDB entry 4b54 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The Escherichia coli Lpt transenvelope protein complex for lipopolysaccharide export is assembled via conserved structurally homologous domains.
Villa R, Martorana AM, Okuda S, Gourlay LJ, Nardini M, Sperandeo P, Dehò G, Bolognesi M, Kahne D, Polissi A
J Bacteriol 195 1100-8 (2013)
PMID: 23292770

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-142383 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipopolysaccharide export system protein LptC Chains: A, B
Molecule details ›
Chains: A, B
Length: 176 amino acids
Theoretical weight: 20.23 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0ADV9 (Residues: 24-191; Coverage: 88%)
Gene names: JW3166, b3199, lptC, yrbK
Sequence domains: Lipopolysaccharide-assembly, LptC-related
Structure domains: Lipopolysaccharide (LPS) transport protein A like domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 40.94Å b: 98.28Å c: 123.56Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.242 0.24 0.266
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

21 review citations

Biosynthesis and export of bacterial lipopolysaccharides.
Whitfield et al. (2014)
20 more

4 mentions without citation

Structural basis of unidirectional export of lipopolysaccharide to the cell surface.
Owens et al. (2019)
3 more