› 1eha

X-ray diffraction
3Å resolution

CRYSTAL STRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS

Released:
DOI: 10.2210/pdb1eha/pdb
PDB entry 1eha coloured by chain, front view.
PDB entry 1eha coloured by chain, side view.
PDB entry 1eha coloured by chain, top view.
Source organism: Saccharolobus solfataricus
Primary publication:
Crystal structure of glycosyltrehalose trehalohydrolase from the hyperthermophilic archaeum Sulfolobus solfataricus.
Feese MD, Kato Y, Tamada T, Kato M, Komeda T, Miura Y, Hirose M, Hondo K, Kobayashi K, Kuroki R
J Mol Biol 301 451-64 (2000)
PMID: 10926520

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 domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176267 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Malto-oligosyltrehalose trehalohydrolase Chain: A
Molecule details ›
Chain: A
Length: 558 amino acids
Theoretical weight: 64.74 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P3221
Unit cell:
a: 80.366Å b: 80.366Å c: 281.998Å
α: 90° β: 90° γ: 120°
Expression system: Cyberlindnera jadinii

Quick links

Citations

2 review citations

Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes.
MacGregor et al. (2001)
1 more

3 mentions without citation

Crystal structure of full-length Mycobacterium tuberculosis H37Rv glycogen branching enzyme: insights of N-terminal beta-sandwich in substrate specificity and enzymatic activity.
Pal et al. (2010)
2 more