› 2pwe

X-ray diffraction
2Å resolution

Crystal structure of the MutB E254Q mutant in complex with the substrate sucrose

Released:
DOI: 10.2210/pdb2pwe/pdb
PDB entry 2pwe coloured by chain, front view.
PDB entry 2pwe coloured by chain, side view.
PDB entry 2pwe coloured by chain, top view.
Source organism: Burkholderia ubonensis subsp. mesacidophila
Primary publication:
Trehalulose synthase native and carbohydrate complexed structures provide insights into sucrose isomerization.
Ravaud S, Robert X, Watzlawick H, Haser R, Mattes R, Aghajari N
J Biol Chem 282 28126-36 (2007)
PMID: 17597061

Function and Biology Details

Reaction catalysed: 
Sucrose = 6-O-alpha-D-glucopyranosyl-D-fructofuranose
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173875 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Glycosyl hydrolase family 13 catalytic domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 556 amino acids
Theoretical weight: 63.81 KDa
Source organism: Burkholderia ubonensis subsp. mesacidophila
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2PS28 (Residues: 29-584; Coverage: 99%)
Gene name: mutB
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, FRU
Carbohydrate polymer
1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P1
Unit cell:
a: 64.31Å b: 73.73Å c: 82.75Å
α: 66.18° β: 74.51° γ: 72.55°
R-values:
R R work R free
0.19 0.19 0.235
Expression system: Escherichia coli

Quick links

Citations

5 review citations

α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.
Janeček et al. (2014)
4 more

5 mentions without citation

The structure of the Mycobacterium smegmatis trehalose synthase reveals an unusual active site configuration and acarbose-binding mode.
Caner et al. (2013)
4 more