› 1mvy

X-ray diffraction
2Å resolution

Amylosucrase mutant E328Q co-crystallized with maltoheptaose.

Released:
DOI: 10.2210/pdb1mvy/pdb
PDB entry 1mvy coloured by chain, front view.
PDB entry 1mvy coloured by chain, side view.
PDB entry 1mvy coloured by chain, top view.
Source organism: Neisseria polysaccharea
Primary publication:
Oligosaccharide and sucrose complexes of amylosucrase. Structural implications for the polymerase activity.
Skov LK, Mirza O, Sprogøe D, Dar I, Remaud-Simeon M, Albenne C, Monsan P, Gajhede M
J Biol Chem 277 47741-7 (2002)
PMID: 12364331

Function and Biology Details

Reaction catalysed: 
Sucrose + ((1->4)-alpha-D-glucosyl)(n) = D-fructose + ((1->4)-alpha-D-glucosyl)(n+1)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195625 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Amylosucrase Chain: A
Molecule details ›
Chain: A
Length: 628 amino acids
Theoretical weight: 71.53 KDa
Source organism: Neisseria polysaccharea
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9ZEU2 (Residues: 13-636; Coverage: 98%)
Gene name: ams
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
1 bound ligand:
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P21212
Unit cell:
a: 96.028Å b: 116.358Å c: 60.303Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 0.217
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Structure-function relationships of glucansucrase and fructansucrase enzymes from lactic acid bacteria.
van Hijum et al. (2006)
4 more

1 mention without citation

Defining structural and evolutionary modules in proteins: a community detection approach to explore sub-domain architecture.
Hleap et al. (2013)