› 3d6e

X-ray diffraction
2.4Å resolution

Crystal structure of the engineered 1,3-1,4-beta-glucanase protein from Bacillus licheniformis

Released:
DOI: 10.2210/pdb3d6e/pdb
PDB entry 3d6e coloured by chain, front view.
PDB entry 3d6e coloured by chain, side view.
PDB entry 3d6e coloured by chain, top view.
Source organism: Bacillus licheniformis
Primary publication:
Re-engineering specificity in 1,3-1, 4-β-glucanase to accept branched xyloglucan substrates.
Addington T, Calisto B, Alfonso-Prieto M, Rovira C, Fita I, Planas A
Proteins 79 365-75 (2011)
PMID: 21069723

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150924 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-glucanase Chains: A, B
Molecule details ›
Chains: A, B
Length: 201 amino acids
Theoretical weight: 22.75 KDa
Source organism: Bacillus licheniformis
Expression system: Escherichia coli
UniProt:
  • Canonical: P27051 (Residues: 30-243; Coverage: 93%)
Gene name: bg1
Sequence domains: Glycosyl hydrolases family 16
Structure domains: Jelly Rolls

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P1
Unit cell:
a: 39.551Å b: 54.813Å c: 54.91Å
α: 61.38° β: 85.72° γ: 86.1°
R-values:
R R work R free
0.213 0.21 0.255
Expression system: Escherichia coli

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Citations

1 review citation

The features that distinguish lichenases from other polysaccharide-hydrolyzing enzymes and the relevance of lichenases for biotechnological applications.
Goldenkova-Pavlova et al. (2018)
5 other articles

2 mentions without citation

Insights into Krabbe disease from structures of galactocerebrosidase.
Deane et al. (2011)
1 more