› 3ph0

X-ray diffraction
2.4Å resolution

Crystal structure of the heteromolecular chaperone, AscE-AscG, from the type III secretion system in Aeromonas hydrophila

Released:
DOI: 10.2210/pdb3ph0/pdb
PDB entry 3ph0 coloured by chain, front view.
PDB entry 3ph0 coloured by chain, side view.
PDB entry 3ph0 coloured by chain, top view.
Source organism: Aeromonas hydrophila
Primary publication:
Crystal structure of the heteromolecular chaperone, AscE-AscG, from the type III secretion system in Aeromonas hydrophila.
Chatterjee C, Kumar S, Chakraborty S, Tan YW, Leung KY, Sivaraman J, Mok YK
OpenAccess logo PLoS One 6 e19208 (2011)
PMID: 21559439

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172816 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
AscE Chains: A, B
Molecule details ›
Chains: A, B
Length: 67 amino acids
Theoretical weight: 7.57 KDa
Source organism: Aeromonas hydrophila
Expression system: Escherichia coli
UniProt:
  • Canonical: Q1EHA4 (Residues: 1-67; Coverage: 100%)
Gene name: ascE
Sequence domains: Type III secretion system, cytoplasmic E component of needle
Structure domains: Immunoglobulin FC, subunit C
AscG Chains: C, D
Molecule details ›
Chains: C, D
Length: 61 amino acids
Theoretical weight: 6.76 KDa
Source organism: Aeromonas hydrophila
Expression system: Escherichia coli
UniProt:
  • Canonical: Q1EHA2 (Residues: 1-61; Coverage: 53%)
Gene name: ascG
Sequence domains: Bacterial type II secretion system chaperone protein (type_III_yscG)
Structure domains: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P21212
Unit cell:
a: 43.159Å b: 71.937Å c: 86.735Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.239 0.292
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria.
Büttner D. (2012)
2 more

2 mentions without citation

Molecular Targets and Strategies for Inhibition of the Bacterial Type III Secretion System (T3SS); Inhibitors Directly Binding to T3SS Components.
Hotinger et al. (2021)
1 more