› 4ce7

X-ray diffraction
1.9Å resolution

Crystal structure of a novel unsaturated beta-glucuronyl hydrolase enzyme, belonging to family GH105, involved in ulvan degradation

Released:
DOI: 10.2210/pdb4ce7/pdb
PDB entry 4ce7 coloured by chain, front view.
PDB entry 4ce7 coloured by chain, side view.
PDB entry 4ce7 coloured by chain, top view.
Source organism: Nonlabens ulvanivorans
Primary publication:
A novel unsaturated β-glucuronyl hydrolase involved in ulvan degradation unveils the versatility of stereochemistry requirements in family GH105.
Collén PN, Jeudy A, Sassi JF, Groisillier A, Czjzek M, Coutinho PM, Helbert W
J Biol Chem 289 6199-211 (2014)
PMID: 24407291

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125830 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Unsaturated 3S-rhamnoglycuronyl hydrolase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 370 amino acids
Theoretical weight: 43.14 KDa
Source organism: Nonlabens ulvanivorans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: L7P9J4 (Residues: 16-377; Coverage: 100%)
Gene name: IL45_01505
Sequence domains: Glycosyl Hydrolase Family 88
Structure domains: Glycosyltransferase

Ligands and Environments

1 bound ligand:
Ligand NO3 4 x NO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 92.978Å b: 93.331Å c: 156.758Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.162 0.207
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

A sweet new wave: structures and mechanisms of enzymes that digest polysaccharides from marine algae.
Hehemann et al. (2014)
3 more

3 mentions without citation

A novel unsaturated β-glucuronyl hydrolase involved in ulvan degradation unveils the versatility of stereochemistry requirements in family GH105.
Collén et al. (2014)
2 more