› 4m9c

X-ray diffraction
2.1Å resolution

WeeI from Acinetobacter baumannii AYE

Released:
DOI: 10.2210/pdb4m9c/pdb
PDB entry 4m9c coloured by chain, front view.
PDB entry 4m9c coloured by chain, side view.
PDB entry 4m9c coloured by chain, top view.
Source organism: Acinetobacter baumannii
Primary publication:
Biochemical analysis and structure determination of bacterial acetyltransferases responsible for the biosynthesis of UDP-N,N'-diacetylbacillosamine.
Morrison MJ, Imperiali B
J Biol Chem 288 32248-32260 (2013)
PMID: 24064219

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-241384 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bacterial transferase hexapeptide (Three repeats) family protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 216 amino acids
Theoretical weight: 22.99 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli BL21(DE3)
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P3121
Unit cell:
a: 148.289Å b: 148.289Å c: 182.413Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.191 0.226
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

The renaissance of bacillosamine and its derivatives: pathway characterization and implications in pathogenicity.
Morrison et al. (2014)
5 other articles

3 mentions without citation

The rare sugar N-acetylated viosamine is a major component of Mimivirus fibers.
Piacente et al. (2017)
2 more