› 2uvi

X-ray diffraction
2.3Å resolution

Structure of a periplasmic oligogalacturonide binding protein from Yersinia enterocolitica in complex with 4,5-unsaturated digalacturonic acid

Released:
DOI: 10.2210/pdb2uvi/pdb
PDB entry 2uvi coloured by chain, front view.
PDB entry 2uvi coloured by chain, side view.
PDB entry 2uvi coloured by chain, top view.
Source organism: Yersinia enterocolitica
Primary publication:
Specific recognition of saturated and 4,5-unsaturated hexuronate sugars by a periplasmic binding protein involved in pectin catabolism.
Abbott DW, Boraston AB
J Mol Biol 369 759-70 (2007)
PMID: 17451747

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163253 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
ABC TYPE PERIPLASMIC SUGAR-BINDING PROTEIN Chain: A
Molecule details ›
Chain: A
Length: 408 amino acids
Theoretical weight: 46.34 KDa
Source organism: Yersinia enterocolitica
Expression system: Escherichia coli
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

Carbohydrate polymer : NEW Components: ADA, AQA
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 68.262Å b: 110.21Å c: 119.394Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.209 0.286
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions.
Eitinger et al. (2011)
2 more

1 mention without citation

Development of a Real-Time Pectic Oligosaccharide-Detecting Biosensor Using the Rapid and Flexible Computational Identification of Non-Disruptive Conjugation Sites (CINC) Biosensor Design Platform.
Smith et al. (2022)