› 1uyp

X-ray diffraction
1.9Å resolution

The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima

Released:
DOI: 10.2210/pdb1uyp/pdb
PDB entry 1uyp coloured by chain, front view.
PDB entry 1uyp coloured by chain, side view.
PDB entry 1uyp coloured by chain, top view.
Source organism: Thermotoga maritima MSB8
Primary publication:
The three-dimensional structure of invertase (beta-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases.
Alberto F, Bignon C, Sulzenbacher G, Henrissat B, Czjzek M
J Biol Chem 279 18903-10 (2004)
PMID: 14973124

Function and Biology Details

Reaction catalysed: 
Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128504 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-fructosidase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 432 amino acids
Theoretical weight: 49.89 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O33833 (Residues: 1-432; Coverage: 100%)
Gene names: TM_1414, bfrA
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand SO4 14 x SO4
Ligand CIT 1 x CIT
Ligand GOL 6 x GOL
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 94.48Å b: 114.67Å c: 130.03Å
α: 90° β: 98.96° γ: 90°
R-values:
R R work R free
0.179 0.177 0.22
Expression system: Escherichia coli BL21

Quick links

Citations

7 review citations

Recent structural insights into the expanding world of carbohydrate-active enzymes.
Davies et al. (2005)
6 more

7 mentions without citation

Structural and kinetic analysis of Schwanniomyces occidentalis invertase reveals a new oligomerization pattern and the role of its supplementary domain in substrate binding.
Alvaro-Benito et al. (2010)
6 more