› 3usz

X-ray diffraction
2.1Å resolution

Crystal structure of truncated exo-1,3/1,4-beta-glucanase (EXOP) from Pseudoalteromonas sp. BB1

Released:
DOI: 10.2210/pdb3usz/pdb
PDB entry 3usz coloured by chain, front view.
PDB entry 3usz coloured by chain, side view.
PDB entry 3usz coloured by chain, top view.
Source organism: Pseudoalteromonas sp. BB1
Primary publication:
Structure and activity of exo-1,3/1,4-β-glucanase from marine bacterium Pseudoalteromonas sp. BB1 showing a novel C-terminal domain.
Nakatani Y, Cutfield SM, Cowieson NP, Cutfield JF
FEBS J 279 464-78 (2012)
PMID: 22129429

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171091 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
beta-glucosidase Chain: A
Molecule details ›
Chain: A
Length: 822 amino acids
Theoretical weight: 90.62 KDa
Source organism: Pseudoalteromonas sp. BB1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q0QJA3 (Residues: 28-840; Coverage: 100%)
Gene name: exoP
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand CA 1 x CA
Ligand NA 1 x NA
Ligand K 1 x K
Ligand EDO 3 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2221
Unit cell:
a: 68.054Å b: 179.414Å c: 177.177Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.164 0.194
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Inactivation and process intensification of β-glucosidase in biomass utilization.
Mu et al. (2023)
19 other articles

1 mention without citation

Structure and activity of exo-1,3/1,4-β-glucanase from marine bacterium Pseudoalteromonas sp. BB1 showing a novel C-terminal domain.
Nakatani et al. (2012)