1xou

X-ray diffraction
2.8Å resolution

Crystal structure of the CesA-EspA complex

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-129372 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Translocon EspA Chain: A
Molecule details ›
Chain: A
Length: 192 amino acids
Theoretical weight: 20.9 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q47184 (Residues: 1-192; Coverage: 100%)
Gene names: D3G36_09190, NCTC10089_00097, espA
Sequence domains: EspA-like secreted protein
Structure domains: EspA/CesA-like
Orf3 Chain: B
Molecule details ›
Chain: B
Length: 95 amino acids
Theoretical weight: 10.81 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O52124 (Residues: 1-95; Coverage: 89%)
Gene names: D4N09_11150, L537_062, LDEC_054, LIHIT_058, orf3
Sequence domains: Type III secretion system filament chaperone CesA
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P212121
Unit cell:
a: 35.422Å b: 72.383Å c: 95.679Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.236 0.265
Expression system: Escherichia coli BL21