› 1dyp

X-ray diffraction
1.54Å resolution

1,3-ALPHA-1,4-BETA-D-GALACTOSE-4-SULFATE-3,6-ANHYDRO-D-GALACTOSE 4 GALACTOHYDROLASE

Released:
DOI: 10.2210/pdb1dyp/pdb
PDB entry 1dyp coloured by chain, front view.
PDB entry 1dyp coloured by chain, side view.
PDB entry 1dyp coloured by chain, top view.
Source organism: Pseudoalteromonas carrageenovora
Primary publication:
The kappa-carrageenase of P. carrageenovora features a tunnel-shaped active site: a novel insight in the evolution of Clan-B glycoside hydrolases.
Michel G, Chantalat L, Duee E, Barbeyron T, Henrissat B, Kloareg B, Dideberg O
Structure 9 513-25 (2001)
PMID: 11435116

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in kappa-carrageenans.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155073 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kappa-carrageenase Chain: A
Molecule details ›
Chain: A
Length: 271 amino acids
Theoretical weight: 31.56 KDa
Source organism: Pseudoalteromonas carrageenovora
Expression system: Escherichia coli
UniProt:
  • Canonical: P43478 (Residues: 27-297; Coverage: 73%)
Gene name: cgkA
Sequence domains: Glycosyl hydrolases family 16
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand CD 7 x CD
Ligand CL 7 x CL
1 modified residue:
Ligand MSE 5 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P212121
Unit cell:
a: 56.408Å b: 61.12Å c: 75.523Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.178 0.193
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Evolution and diversity of plant cell walls: from algae to flowering plants.
Popper et al. (2011)
11 more

9 mentions without citation

Molecular modeling of family GH16 glycoside hydrolases: potential roles for xyloglucan transglucosylases/hydrolases in cell wall modification in the poaceae.
Strohmeier et al. (2004)
8 more