› 3vge

X-ray diffraction
2.7Å resolution

Crystal structure of glycosyltrehalose trehalohydrolase (D252S)

Released:
DOI: 10.2210/pdb3vge/pdb
PDB entry 3vge coloured by chain, front view.
PDB entry 3vge coloured by chain, side view.
PDB entry 3vge coloured by chain, top view.
Source organism: Saccharolobus solfataricus
Primary publication:
Substrate recognition mechanism of a glycosyltrehalose trehalohydrolase from Sulfolobus solfataricus KM1.
Okazaki N, Tamada T, Feese MD, Kato M, Miura Y, Komeda T, Kobayashi K, Kondo K, Blaber M, Kuroki R
Protein Sci 21 539-52 (2012)
PMID: 22334583

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-((1->4)-alpha-D-glucanosyl)(n) trehalose to yield trehalose and (1->4)-alpha-D-glucan
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-176266 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Malto-oligosyltrehalose trehalohydrolase Chain: A
Molecule details ›
Chain: A
Length: 558 amino acids
Theoretical weight: 64.71 KDa
Source organism: Saccharolobus solfataricus
Expression system: Cyberlindnera jadinii
UniProt:
  • Canonical: Q55088 (Residues: 2-559; Coverage: 100%)
Gene name: treZ
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand FLC 1 x FLC
Ligand GOL 7 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P3221
Unit cell:
a: 78.506Å b: 78.506Å c: 282.444Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.162 0.159 0.212
Expression system: Cyberlindnera jadinii

Quick links

Citations

1 citations in other articles

Crystal structure of glycosyltrehalose synthase from Sulfolobus shibatae DSM5389.
Okazaki et al. (2018)

1 mention without citation

An Algorithm for Protein Helix Assignment Using Helix Geometry.
Cao et al. (2015)