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X-ray diffraction
2.55Å resolution

Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with 2-deoxy-2-fluoro-alpha-D-glucoside

Released:
DOI: 10.2210/pdb1iew/pdb
PDB 1iew coloured by chain and viewed from the front.
PDB 1iew coloured by chain and viewed from the side.
PDB 1iew coloured by chain and viewed from the top.
Source organism: Hordeum vulgare
Primary publication:
Catalytic mechanisms and reaction intermediates along the hydrolytic pathway of a plant beta-D-glucan glucohydrolase.
Hrmova M, Varghese JN, De Gori R, Smith BJ, Driguez H, Fincher GB
Structure 9 1005-16 (2001)
PMID: 11709165

Function and Biology Details

Reaction catalysed: 
Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Beta-D-glucan exohydrolase isoenzyme ExoI Chain: A
Molecule details ›
Chain: A
Length: 605 amino acids
Theoretical weight: 65.48 KDa
Source organism: Hordeum vulgare
UniProt:
  • Canonical: Q9XEI3 (Residues: 26-630; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN, FUL
Carbohydrate polymer
2 bound ligands:
Ligand NAG 1 x NAG
Ligand G2F 1 x G2F
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE
Spacegroup: P43212
Unit cell:
a: 100.962Å b: 100.962Å c: 181.254Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.233

Quick links

Citations

5 review citations

A historical perspective for the catalytic reaction mechanism of glycosidase; so as to bring about breakthrough in confusing situation.
Chiba S. (2012)
4 more

2 mentions without citation

Crystallisation of wild-type and variant forms of a recombinant plant enzyme β-D-glucan glucohydrolase from barley (Hordeum vulgare L.) and preliminary X-ray analysis.
Luang et al. (2010)
1 more