› 2xcu

X-ray diffraction
2.42Å resolution

Membrane-embedded monofunctional glycosyltransferase WaaA of Aquifex aeolicus, complex with CMP

Released:
DOI: 10.2210/pdb2xcu/pdb
PDB entry 2xcu coloured by chain, front view.
PDB entry 2xcu coloured by chain, side view.
PDB entry 2xcu coloured by chain, top view.
Source organism: Aquifex aeolicus
Primary publication:
Structural and mechanistic analysis of the membrane-embedded glycosyltransferase WaaA required for lipopolysaccharide synthesis.
Schmidt H, Hansen G, Singh S, Hanuszkiewicz A, Lindner B, Fukase K, Woodard RW, Holst O, Hilgenfeld R, Mamat U, Mesters JR
Proc Natl Acad Sci U S A 109 6253-8 (2012)
PMID: 22474366

Function and Biology Details

Reaction catalysed: 
A lipid IV(A) + CMP-beta-Kdo = an alpha-Kdo-(2->6)-lipid IV(A) + CMP
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130361 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-deoxy-D-manno-octulosonic acid transferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 374 amino acids
Theoretical weight: 43.28 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O66663 (Residues: 1-353; Coverage: 100%)
Gene names: aq_326, kdtA
Sequence domains: 3-Deoxy-D-manno-octulosonic-acid transferase (kdotransferase)
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand C5P 4 x C5P
Ligand 1PE 4 x 1PE
Ligand CIT 5 x CIT
Ligand BME 4 x BME
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: P21
Unit cell:
a: 131.77Å b: 44.67Å c: 143.64Å
α: 90° β: 97.15° γ: 90°
R-values:
R R work R free
0.205 0.202 0.251
Expression system: Escherichia coli BL21

Quick links

Citations

13 review citations

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

5 mentions without citation

Current Progress in the Structural and Biochemical Characterization of Proteins Involved in the Assembly of Lipopolysaccharide.
Bohl et al. (2018)
4 more