› 2iua

X-ray diffraction
2.7Å resolution

C. trachomatis LpxD

Released:
DOI: 10.2210/pdb2iua/pdb
PDB entry 2iua coloured by chain, front view.
PDB entry 2iua coloured by chain, side view.
PDB entry 2iua coloured by chain, top view.
Source organism: Chlamydia trachomatis
Primary publication:
Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis.
Buetow L, Smith TK, Dawson A, Fyffe S, Hunter WN
Proc Natl Acad Sci U S A 104 4321-6 (2007)
PMID: 17360522

Function and Biology Details

Reaction catalysed: 
A (3R)-3-hydroxyacyl-[acyl-carrier-protein] + a UDP-3-O-((3R)-hydroxyacyl)-alpha-D-glucosamine = a UDP-2-N,3-O-bis((3R)-3-hydroxyacyl)-alpha-D-glucosamine + a holo-[acyl-carrier-protein]
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143204 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-3-O-acylglucosamine N-acyltransferase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 374 amino acids
Theoretical weight: 40.63 KDa
Source organism: Chlamydia trachomatis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0CD76 (Residues: 1-354; Coverage: 100%)
Gene names: CT_243, lpxD
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MES 1 x MES
Ligand SO4 8 x SO4
Ligand PLM 3 x PLM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P41212
Unit cell:
a: 98.679Å b: 98.679Å c: 284.505Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.209 0.273
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

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

5 mentions without citation

Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis.
Buetow et al. (2007)
4 more