› 4mad

X-ray diffraction
1.8Å resolution

Crystal structure of beta-galactosidase C (BgaC) from Bacillus circulans ATCC 31382

Released:
DOI: 10.2210/pdb4mad/pdb
PDB entry 4mad coloured by chain, front view.
PDB entry 4mad coloured by chain, side view.
PDB entry 4mad coloured by chain, top view.
Source organism: Niallia circulans
Primary publication:
Rational design of a glycosynthase by the crystal structure of β-galactosidase from Bacillus circulans (BgaC) and its use for the synthesis of N-acetyllactosamine type 1 glycan structures.
Henze M, You DJ, Kamerke C, Hoffmann N, Angkawidjaja C, Ernst S, Pietruszka J, Kanaya S, Elling L
J Biotechnol 191 78-85 (2014)
PMID: 25034434

Function and Biology Details

Reaction catalysed: 
Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128281 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-galactosidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 600 amino acids
Theoretical weight: 68.58 KDa
Source organism: Niallia circulans
Expression system: Escherichia coli
UniProt:
  • Canonical: O31341 (Residues: 1-586; Coverage: 100%)
Gene name: bgaC
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand PG0 3 x PG0
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: C2
Unit cell:
a: 143.268Å b: 93.122Å c: 119.567Å
α: 90° β: 125.67° γ: 90°
R-values:
R R work R free
0.183 0.181 0.216
Expression system: Escherichia coli

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Citations

3 review citations

Cold-Active β-Galactosidases: Insight into Cold Adaption Mechanisms and Biotechnological Exploitation.
Mangiagalli et al. (2021)
2 more

4 mentions without citation

Structural Insights into the Molecular Evolution of the Archaeal Exo-β-d-Glucosaminidase.
Mine et al. (2019)
3 more