› 2x2i

X-ray diffraction
2.6Å resolution

Crystal structure of the Gracilariopsis lemaneiformis alpha-1,4- glucan lyase with acarbose

Released:
DOI: 10.2210/pdb2x2i/pdb
PDB entry 2x2i coloured by chain, front view.
PDB entry 2x2i coloured by chain, side view.
PDB entry 2x2i coloured by chain, top view.
Source organism: Gracilariopsis lemaneiformis
Primary publication:
Crystal structure of α-1,4-glucan lyase, a unique glycoside hydrolase family member with a novel catalytic mechanism.
Rozeboom HJ, Yu S, Madrid S, Kalk KH, Zhang R, Dijkstra BW
J Biol Chem 288 26764-74 (2013)
PMID: 23902768

Function and Biology Details

Reaction catalysed: 
Linear alpha-glucan = (n-1) 1,5-anhydro-D-fructose + D-glucose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193531 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Glucosidase II subunit alpha Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 1027 amino acids
Theoretical weight: 116.06 KDa
Source organism: Gracilariopsis lemaneiformis
Expression system: Ogataea polymorpha RB11
UniProt:
  • Canonical: Q9STC1 (Residues: 62-1088; Coverage: 94%)
Gene name: Ag111
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, GLC, AC1
Ligand BGC 8 x BGC
Ligand GLC 8 x GLC
Ligand AC1 8 x AC1
1 bound ligand:
Ligand GOL 7 x GOL
1 modified residue:
Ligand CSO 4 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P21
Unit cell:
a: 134.861Å b: 91.804Å c: 193.349Å
α: 90° β: 99.34° γ: 90°
R-values:
R R work R free
0.234 0.229 0.32
Expression system: Ogataea polymorpha RB11

Quick links

Citations

2 review citations

α-Glucosidases and α-1,4-glucan lyases: structures, functions, and physiological actions.
Okuyama et al. (2016)
1 more

2 mentions without citation

Molecular basis for the recognition of long-chain substrates by plant α-glucosidases.
Tagami et al. (2013)
1 more