› 1k3e

X-ray diffraction
2.8Å resolution

Type III secretion chaperone CesT

Released:
DOI: 10.2210/pdb1k3e/pdb
Model geometry
Fit model/data
PDB entry 1k3e coloured by chain, front view.
PDB entry 1k3e coloured by chain, side view.
PDB entry 1k3e coloured by chain, top view.
Source organism: Escherichia coli O157:H7
Primary publication:
Structural and biochemical characterization of the type III secretion chaperones CesT and SigE.
Luo Y, Bertero MG, Frey EA, Pfuetzner RA, Wenk MR, Creagh L, Marcus SL, Lim D, Sicheri F, Kay C, Haynes C, Finlay BB, Strynadka NC
Nat Struct Biol 8 1031-6 (2001)
PMID: 11685226

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157660 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tir chaperone Chains: A, B
Molecule details ›
Chains: A, B
Length: 156 amino acids
Theoretical weight: 17.69 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P58233 (Residues: 1-156; Coverage: 100%)
Gene names: ECs4560, L0026, Z5111, cesT
Sequence domains: Tir chaperone protein (CesT) family
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 57.586Å b: 77.856Å c: 94.176Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.225 0.285
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

20 review citations

The type III secretion injectisome.
Cornelis GR. (2006)
19 more

10 mentions without citation

Process of protein transport by the type III secretion system.
Ghosh P. (2004)
9 more