› 2gdu

X-ray diffraction
2.1Å resolution

E232Q mutant of sucrose phosphorylase from BIFIDOBACTERIUM ADOLESCENTIS in complex with sucrose

Released:
DOI: 10.2210/pdb2gdu/pdb
PDB entry 2gdu coloured by chain, front view.
PDB entry 2gdu coloured by chain, side view.
PDB entry 2gdu coloured by chain, top view.
Source organism: Bifidobacterium adolescentis
Primary publication:
Structural rearrangements of sucrose phosphorylase from Bifidobacterium adolescentis during sucrose conversion.
Mirza O, Skov LK, Sprogøe D, van den Broek LA, Beldman G, Kastrup JS, Gajhede M
J Biol Chem 281 35576-84 (2006)
PMID: 16990265

Function and Biology Details

Reaction catalysed: 
Sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106526 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Sucrose phosphorylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 504 amino acids
Theoretical weight: 56.28 KDa
Source organism: Bifidobacterium adolescentis
Expression system: Escherichia coli
UniProt:
  • Canonical: A0ZZH6 (Residues: 1-504; Coverage: 100%)
Gene names: BAD_0078, spl, sucP
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, FRU
Carbohydrate polymer
No bound ligands
1 modified residue:
Ligand CSD 2 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P212121
Unit cell:
a: 55.331Å b: 124.157Å c: 152.453Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.182 0.217
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Bifidobacterium carbohydrases-their role in breakdown and synthesis of (potential) prebiotics.
van den Broek et al. (2008)
6 more

10 mentions without citation

Discovery and Biotechnological Exploitation of Glycoside-Phosphorylases.
Li et al. (2022)
9 more