› 3qom

X-ray diffraction
1.5Å resolution

Crystal structure of 6-phospho-beta-glucosidase from Lactobacillus plantarum

Released:
DOI: 10.2210/pdb3qom/pdb
PDB entry 3qom coloured by chain, front view.
PDB entry 3qom coloured by chain, side view.
PDB entry 3qom coloured by chain, top view.
Source organism: Lactiplantibacillus plantarum
Primary publication:
GH1-family 6-P-β-glucosidases from human microbiome lactic acid bacteria.
Michalska K, Tan K, Li H, Hatzos-Skintges C, Bearden J, Babnigg G, Joachimiak A
OpenAccess logo Acta Crystallogr D Biol Crystallogr 69 451-63 (2013)
PMID: 23519420

Function and Biology Details

Reaction catalysed: 
6-phospho-beta-D-glucosyl-(1,4)-D-glucose + H(2)O = D-glucose + D-glucose 6-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123807 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
6-phospho-beta-glucosidase Chain: A
Molecule details ›
Chain: A
Length: 481 amino acids
Theoretical weight: 55.81 KDa
Source organism: Lactiplantibacillus plantarum
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: F9UU25 (Residues: 1-478; Coverage: 100%)
Gene names: lp_0440, pbg1
Sequence domains: Glycosyl hydrolase family 1
Structure domains: Glycosidases

Ligands and Environments

3 bound ligands:
Ligand BGC 1 x BGC
Ligand PO4 4 x PO4
Ligand ACT 1 x ACT
1 modified residue:
Ligand MSE 13 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P622
Unit cell:
a: 150.647Å b: 150.647Å c: 95.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.118 0.118 0.134
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

β-Glucosidase activities of lactic acid bacteria: mechanisms, impact on fermented food and human health.
Michlmayr et al. (2014)
1 more

4 mentions without citation

Transcriptional analysis of prebiotic uptake and catabolism by Lactobacillus acidophilus NCFM.
Andersen et al. (2012)
3 more