› 1o6t

X-ray diffraction
1.6Å resolution

Internalin (INLA, Listeria monocytogenes) - functional domain, uncomplexed

Released:
DOI: 10.2210/pdb1o6t/pdb
PDB entry 1o6t coloured by chain, front view.
PDB entry 1o6t coloured by chain, side view.
PDB entry 1o6t coloured by chain, top view.
Source organism: Listeria monocytogenes EGD-e
Primary publication:
Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin.
Schubert WD, Urbanke C, Ziehm T, Beier V, Machner MP, Domann E, Wehland J, Chakraborty T, Heinz DW
Cell 111 825-36 (2002)
PMID: 12526809

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143597 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Internalin A Chain: A
Molecule details ›
Chain: A
Length: 466 amino acids
Theoretical weight: 50.24 KDa
Source organism: Listeria monocytogenes EGD-e
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0DJM0 (Residues: 36-496; Coverage: 60%)
Gene names: inlA, lmo0433
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand MG 1 x MG
Ligand CA 1 x CA
Ligand CL 2 x CL
Ligand SO4 4 x SO4
Ligand MES 5 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: C2
Unit cell:
a: 95.919Å b: 55.881Å c: 97.78Å
α: 90° β: 113.07° γ: 90°
R-values:
R R work R free
0.133 0.131 0.161
Expression system: Escherichia coli BL21

Quick links

Citations

59 review citations

Sortases and the art of anchoring proteins to the envelopes of gram-positive bacteria.
Marraffini et al. (2006)
58 more