› 3rwk

X-ray diffraction
2.1Å resolution

First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes.

Released:
DOI: 10.2210/pdb3rwk/pdb
PDB entry 3rwk coloured by chain, front view.
PDB entry 3rwk coloured by chain, side view.
PDB entry 3rwk coloured by chain, top view.
Source organism: Aspergillus ficuum
Primary publication:
First crystal structure of an endo-inulinase, INU2, from Aspergillus ficuum: discovery of an extra-pocket in the catalytic domain responsible for its endo-activity.
Pouyez J, Mayard A, Vandamme AM, Roussel G, Perpète EA, Wouters J, Housen I, Michaux C
Biochimie 94 2423-30 (2012)
PMID: 22750808

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (2->1)-beta-D-fructosidic linkages in inulin
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131698 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Extracellular endo-inulinase inu2 Chain: X
Molecule details ›
Chain: X
Length: 516 amino acids
Theoretical weight: 55.83 KDa
Source organism: Aspergillus ficuum
UniProt:
  • Canonical: O94220 (Residues: 1-516; Coverage: 100%)
Gene name: inu2
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
4 bound ligands:
Ligand FRU 2 x FRU
Ligand NA 1 x NA
Ligand SO4 1 x SO4
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P3121
Unit cell:
a: 95.76Å b: 95.76Å c: 130.82Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.183 0.232

Quick links

Citations

14 citation in other articles

Three-dimensional structure of Saccharomyces invertase: role of a non-catalytic domain in oligomerization and substrate specificity.
Sainz-Polo et al. (2013)
13 more

2 mentions without citation

A Highly Active Endo-Levanase BT1760 of a Dominant Mammalian Gut Commensal Bacteroides thetaiotaomicron Cleaves Not Only Various Bacterial Levans, but Also Levan of Timothy Grass.
Mardo et al. (2017)
1 more