› 6r5t

X-ray diffraction
1.6Å resolution

The crystal structure of Glycoside Hydrolase BglX inactive mutant D286N from P. aeruginosa in complex with lactose

Released:
DOI: 10.2210/pdb6r5t/pdb
PDB entry 6r5t coloured by chain, front view.
PDB entry 6r5t coloured by chain, side view.
PDB entry 6r5t coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Catalytic Cycle of Glycoside Hydrolase BglX from Pseudomonas aeruginosa and Its Implications for Biofilm Formation.
Mahasenan KV, Batuecas MT, De Benedetti S, Kim C, Rana N, Lee M, Hesek D, Fisher JF, Sanz-Aparicio J, Hermoso JA, Mobashery S
ACS Chem Biol 15 189-196 (2020)
PMID: 31877028

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-191313 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
beta-glucosidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 733 amino acids
Theoretical weight: 80.15 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9I311 (Residues: 32-764; Coverage: 99%)
Gene names: PA1726, bglX
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, GAL
Carbohydrate polymer
3 bound ligands:
Ligand PEG 4 x PEG
Ligand MG 2 x MG
Ligand PGE 1 x PGE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P1
Unit cell:
a: 70.978Å b: 73.588Å c: 81.124Å
α: 65.55° β: 73.42° γ: 69.68°
R-values:
R R work R free
0.141 0.139 0.168
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Weaving of bacterial cellulose by the Bcs secretion systems.
Abidi et al. (2022)
1 more