› 4mee

X-ray diffraction
3Å resolution

Crystal structure of the transport unit of the autotransporter AIDA-I from Escherichia coli

Released:
DOI: 10.2210/pdb4mee/pdb
PDB entry 4mee coloured by chain, front view.
PDB entry 4mee coloured by chain, side view.
PDB entry 4mee coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of the transport unit of the autotransporter adhesin involved in diffuse adherence from Escherichia coli.
Gawarzewski I, DiMaio F, Winterer E, Tschapek B, Smits SHJ, Jose J, Schmitt L
J Struct Biol 187 20-29 (2014)
PMID: 24841284

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169853 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AIDA-I translocator Chain: A
Molecule details ›
Chain: A
Length: 469 amino acids
Theoretical weight: 50.95 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: Q03155 (Residues: 840-1286; Coverage: 36%)
Gene names: aidA, aidA-I
Sequence domains: Autochaperone Domain Type 1
Structure domains: Autotransporter beta-domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P212121
Unit cell:
a: 40.33Å b: 85.85Å c: 134.05Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.251 0.248 0.306
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Bacterial whole-cell biocatalysts by surface display of enzymes: toward industrial application.
Schüürmann et al. (2014)
3 more

3 mentions without citation

Of linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion.
Drobnak et al. (2015)
2 more