› 2ix9

X-ray diffraction
1.7Å resolution

Respective role of protein folding and glycosylation in the thermal stability of recombinant Feruloyl Esterase A

Released:
DOI: 10.2210/pdb2ix9/pdb
PDB entry 2ix9 coloured by chain, front view.
PDB entry 2ix9 coloured by chain, side view.
PDB entry 2ix9 coloured by chain, top view.
Source organism: Aspergillus niger
Primary publication:
Respective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A.
Benoit I, Asther M, Sulzenbacher G, Record E, Marmuse L, Parsiegla G, Gimbert I, Asther M, Bignon C
FEBS Lett 580 5815-21 (2006)
PMID: 17027758

Function and Biology Details

Reaction catalysed: 
Feruloyl-polysaccharide + H(2)O = ferulate + polysaccharide
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128815 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Feruloyl esterase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 260 amino acids
Theoretical weight: 28.37 KDa
Source organism: Aspergillus niger
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O42807 (Residues: 22-281; Coverage: 100%)
Gene name: faeA
Sequence domains: Lipase (class 3)
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
Ligand CXS 2 x CXS
Ligand EDO 8 x EDO
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: C2
Unit cell:
a: 158.825Å b: 51.556Å c: 72.553Å
α: 90° β: 109.27° γ: 90°
R-values:
R R work R free
0.155 0.153 0.19
Expression system: Escherichia coli BL21(DE3)

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Citations

5 review citations

Diversity of fungal feruloyl esterases: updated phylogenetic classification, properties, and industrial applications.
Dilokpimol et al. (2016)
4 more