› 1bap

X-ray diffraction
1.75Å resolution

A PRO TO GLY MUTATION IN THE HINGE OF THE ARABINOSE-BINDING PROTEIN ENHANCES BINDING AND ALTERS SPECIFICITY: SUGAR-BINDING AND CRYSTALLOGRAPHIC STUDIES

Released:
DOI: 10.2210/pdb1bap/pdb
PDB entry 1bap coloured by chain, front view.
PDB entry 1bap coloured by chain, side view.
PDB entry 1bap coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
A Pro to Gly mutation in the hinge of the arabinose-binding protein enhances binding and alters specificity. Sugar-binding and crystallographic studies.
Vermersch PS, Tesmer JJ, Lemon DD, Quiocho FA
J Biol Chem 265 16592-603 (1990)
PMID: 2204627

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136385 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-arabinose-binding periplasmic protein Chain: A
Molecule details ›
Chain: A
Length: 306 amino acids
Theoretical weight: 33.21 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P02924 (Residues: 24-329; Coverage: 100%)
Gene names: JW1889, araF, b1901
Sequence domains: Periplasmic binding proteins and sugar binding domain of LacI family
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:
Ligand ARA 1 x ARA
Ligand ARB 1 x ARB
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 55.46Å b: 71.82Å c: 77.84Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 not available not available
Expression system: Not provided

Quick links

Citations

2 review citations

Functions of the gene products of Escherichia coli.
Riley M. (1993)
1 more

3 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
2 more