› 2vyo

X-ray diffraction
1.5Å resolution

Chitin deacetylase family member from Encephalitozoon cuniculi

Released:
DOI: 10.2210/pdb2vyo/pdb
PDB entry 2vyo coloured by chain, front view.
PDB entry 2vyo coloured by chain, side view.
PDB entry 2vyo coloured by chain, top view.
Source organism: Encephalitozoon cuniculi GB-M1
Primary publication:
Structural and functional characterization of a putative polysaccharide deacetylase of the human parasite Encephalitozoon cuniculi.
Urch JE, Hurtado-Guerrero R, Brosson D, Liu Z, Eijsink VG, Texier C, van Aalten DM
Protein Sci 18 1197-209 (2009)
PMID: 19472335

Function and Biology Details

Reaction catalysed: 
Chitin + H(2)O = chitosan + acetate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186102 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Polysaccharide deacetylase domain-containing protein ECU11_0510 Chain: A
Molecule details ›
Chain: A
Length: 254 amino acids
Theoretical weight: 28.16 KDa
Source organism: Encephalitozoon cuniculi GB-M1
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q8SU65 (Residues: 1-254; Coverage: 100%)
Gene name: ECU11_0510
Sequence domains: Polysaccharide deacetylase
Structure domains: Glycoside hydrolase/deacetylase

Ligands and Environments

6 bound ligands:
Ligand CA 4 x CA
Ligand ZN 2 x ZN
Ligand ACT 1 x ACT
Ligand CL 1 x CL
Ligand IMD 1 x IMD
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21212
Unit cell:
a: 64.975Å b: 81.916Å c: 39.201Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.215
Expression system: Komagataella pastoris

Quick links

Citations

3 review citations

Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: an update for 2009-2010.
Harvey DJ. (2015)
2 more

10 mentions without citation

Enzymatic modifications of exopolysaccharides enhance bacterial persistence.
Whitfield et al. (2015)
9 more