› 3wnk

X-ray diffraction
2.3Å resolution

Crystal Structure of Bacillus circulans T-3040 cycloisomaltooligosaccharide glucanotransferase

Released:
DOI: 10.2210/pdb3wnk/pdb
PDB entry 3wnk coloured by chain, front view.
PDB entry 3wnk coloured by chain, side view.
PDB entry 3wnk coloured by chain, top view.
Source organism: Niallia circulans
Primary publication:
Structural elucidation of the cyclization mechanism of α-1,6-glucan by Bacillus circulans T-3040 cycloisomaltooligosaccharide glucanotransferase.
Suzuki N, Fujimoto Z, Kim YM, Momma M, Kishine N, Suzuki R, Suzuki S, Kitamura S, Kobayashi M, Kimura A, Funane K
J Biol Chem 289 12040-12051 (2014)
PMID: 24616103

Function and Biology Details

Reaction catalysed: 
Cyclizes part of a (1->6)-alpha-D-glucan chain by formation of a (1->6)-alpha-D-glucosidic bond
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161097 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cycloisomaltooligosaccharide glucanotransferase Chain: A
Molecule details ›
Chain: A
Length: 721 amino acids
Theoretical weight: 80.22 KDa
Source organism: Niallia circulans
Expression system: Escherichia coli
UniProt:
  • Canonical: P94286 (Residues: 39-738; Coverage: 75%)
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand CD 10 x CD
Ligand CA 2 x CA
Ligand NA 2 x NA
Ligand ACT 2 x ACT
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P3121
Unit cell:
a: 106.437Å b: 106.437Å c: 160.625Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.159 0.158 0.192
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Using structure to inform carbohydrate binding module function.
Abbott et al. (2014)
2 more

6 mentions without citation

Molecular mechanism of Aspergillus fumigatus biofilm disruption by fungal and bacterial glycoside hydrolases.
Le Mauff et al. (2019)
5 more