› 4flr

X-ray diffraction
2.4Å resolution

Crystal structure of Amylosucrase double mutant A289P-F290L from Neisseria polysaccharea

Released:
DOI: 10.2210/pdb4flr/pdb
PDB entry 4flr coloured by chain, front view.
PDB entry 4flr coloured by chain, side view.
PDB entry 4flr coloured by chain, top view.
Source organism: Neisseria polysaccharea
Primary publication:
Applying pairwise combinations of amino acid mutations for sorting out highly efficient glucosylation tools for chemo-enzymatic synthesis of bacterial oligosaccharides.
Champion E, Guérin F, Moulis C, Barbe S, Tran TH, Morel S, Descroix K, Monsan P, Mourey L, Mulard LA, Tranier S, Remaud-Siméon M, André I
J Am Chem Soc 134 18677-88 (2012)
PMID: 23072374

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195625 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amylosucrase Chain: A
Molecule details ›
Chain: A
Length: 628 amino acids
Theoretical weight: 71.56 KDa
Source organism: Neisseria polysaccharea
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9ZEU2 (Residues: 13-636; Coverage: 98%)
Gene name: ams
Sequence domains: Alpha amylase, catalytic domain
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand TRS 1 x TRS
Ligand GOL 18 x GOL
Ligand 1PE 1 x 1PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21212
Unit cell:
a: 96.02Å b: 116.35Å c: 60.17Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.182 0.236
Expression system: Escherichia coli

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Citations

6 review citations

Strategies for the discovery and engineering of enzymes for biocatalysis.
Davids et al. (2013)
5 more