› 1o6v

X-ray diffraction
1.5Å resolution

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

Released:
DOI: 10.2210/pdb1o6v/pdb
PDB entry 1o6v coloured by chain, front view.
PDB entry 1o6v coloured by chain, side view.
PDB entry 1o6v 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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143595 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Internalin A Chains: A, B
Molecule details ›
Chains: A, B
Length: 466 amino acids
Theoretical weight: 50.24 KDa
Source organism: Listeria monocytogenes EGD-e
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0DJM0 (Residues: 35-496; Coverage: 60%)
Gene names: inlA, lmo0433
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: C2
Unit cell:
a: 85.589Å b: 67.907Å c: 154.251Å
α: 90° β: 103.48° γ: 90°
R-values:
R R work R free
0.147 0.145 0.184
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

9 mentions without citation

Simple mechanisms for the evolution of protein complexity.
Pillai et al. (2022)
8 more