› 4zo7

X-ray diffraction
2Å resolution

Crystal structure of mutant (D270A) beta-glucosidase from Listeria innocua in complex with gentiobiose

Released:
DOI: 10.2210/pdb4zo7/pdb
PDB entry 4zo7 coloured by chain, front view.
PDB entry 4zo7 coloured by chain, side view.
PDB entry 4zo7 coloured by chain, top view.
Source organism: Listeria innocua Clip11262
Primary publication:
Functional and Structural Analysis of a β-Glucosidase Involved in β-1,2-Glucan Metabolism in Listeria innocua.
Nakajima M, Yoshida R, Miyanaga A, Abe K, Takahashi Y, Sugimoto N, Toyoizumi H, Nakai H, Kitaoka M, Taguchi H
PLoS One 11 e0148870 (2016)
PMID: 26886583

Function and Biology Details

Reaction catalysed: 
Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187846 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
beta-glucosidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 731 amino acids
Theoretical weight: 80.57 KDa
Source organism: Listeria innocua Clip11262
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92AS9 (Residues: 1-723; Coverage: 100%)
Gene name: lin1840
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, GLC
Carbohydrate polymer
4 bound ligands:
Ligand BGC 3 x BGC
Ligand MG 2 x MG
Ligand GOL 1 x GOL
Ligand GLC 1 x GLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Unit cell:
a: 89.6Å b: 95.16Å c: 215.404Å
α: 90° β: 96.38° γ: 90°
R-values:
R R work R free
0.166 0.163 0.235
Expression system: Escherichia coli

Quick links

Citations

2 review citations

A glucotolerant β-glucosidase from the fungus Talaromyces amestolkiae and its conversion into a glycosynthase for glycosylation of phenolic compounds.
Méndez-Líter et al. (2020)
1 more

1 mention without citation

Mechanisms of redundancy and specificity of the Aspergillus fumigatus Crh transglycosylases.
Fang et al. (2019)