› 1hl8

X-ray diffraction
2.4Å resolution

CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE

Released:
DOI: 10.2210/pdb1hl8/pdb
PDB entry 1hl8 coloured by chain, front view.
PDB entry 1hl8 coloured by chain, side view.
PDB entry 1hl8 coloured by chain, top view.
Source organism: Thermotoga maritima MSB8
Primary publication:
Crystal structure of Thermotoga maritima alpha-L-fucosidase. Insights into the catalytic mechanism and the molecular basis for fucosidosis.
Sulzenbacher G, Bignon C, Nishimura T, Tarling CA, Withers SG, Henrissat B, Bourne Y
J Biol Chem 279 13119-28 (2004)
PMID: 14715651

Function and Biology Details

Reaction catalysed: 
An alpha-L-fucoside + H(2)O = L-fucose + an alcohol
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194507 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-L-fucosidase, putative Chains: A, B
Molecule details ›
Chains: A, B
Length: 449 amino acids
Theoretical weight: 52.32 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9WYE2 (Residues: 1-449; Coverage: 100%)
Gene name: TM_0306
Sequence domains: Alpha-L-fucosidase
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand KCX 2 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: R32
Unit cell:
a: 172.462Å b: 172.462Å c: 167.414Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.185 0.228
Expression system: Escherichia coli BL21

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Citations

8 review citations

Mechanistic insights into glycosidase chemistry.
Vocadlo et al. (2008)
7 more

10 mentions without citation

The dual role of fucosidases: tool or target.
Jiménez-Pérez et al. (2023)
9 more