› 1l8n

X-ray diffraction
1.5Å resolution

The 1.5A crystal structure of alpha-D-glucuronidase from Bacillus stearothermophilus T-1, complexed with 4-O-methyl-glucuronic acid and xylotriose

Released:
DOI: 10.2210/pdb1l8n/pdb
PDB entry 1l8n coloured by chain, front view.
PDB entry 1l8n coloured by chain, side view.
PDB entry 1l8n coloured by chain, top view.
Source organism: Geobacillus stearothermophilus
Primary publication:
Crystal structures of Geobacillus stearothermophilus alpha-glucuronidase complexed with its substrate and products: mechanistic implications.
Golan G, Shallom D, Teplitsky A, Zaide G, Shulami S, Baasov T, Stojanoff V, Thompson A, Shoham Y, Shoham G
J Biol Chem 279 3014-24 (2004)
PMID: 14573597

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->2)-alpha-D-(4-O-methyl)glucuronosyl links in the main chain of hardwood xylans
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-570597 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Xylan alpha-1,2-glucuronidase Chain: A
Molecule details ›
Chain: A
Length: 679 amino acids
Theoretical weight: 78.58 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8VVD2 (Residues: 1-679; Coverage: 100%)
Gene name: aguA
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: XYP
Carbohydrate polymer
2 bound ligands:
Ligand GCW 1 x GCW
Ligand GOL 14 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P41212
Unit cell:
a: 73.946Å b: 73.946Å c: 331.341Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.14 0.14 0.172
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

A mini review of xylanolytic enzymes with regards to their synergistic interactions during hetero-xylan degradation.
Malgas et al. (2019)
1 more

5 mentions without citation

Comparative systems analysis of the secretome of the opportunistic pathogen Aspergillus fumigatus and other Aspergillus species.
Vivek-Ananth et al. (2018)
4 more