› 1qvb

X-ray diffraction
2.4Å resolution

CRYSTAL STRUCTURE OF THE BETA-GLYCOSIDASE FROM THE HYPERTHERMOPHILE THERMOSPHAERA AGGREGANS

Released:
DOI: 10.2210/pdb1qvb/pdb
PDB entry 1qvb coloured by chain, front view.
PDB entry 1qvb coloured by chain, side view.
PDB entry 1qvb coloured by chain, top view.
Source organism: Thermosphaera aggregans
Primary publication:
Crystal structure of the beta-glycosidase from the hyperthermophile Thermosphaera aggregans: insights into its activity and thermostability.
Chi YI, Martinez-Cruz LA, Jancarik J, Swanson RV, Robertson DE, Kim SH
FEBS Lett 445 375-83 (1999)
PMID: 10094493

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195500 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-glycosidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 481 amino acids
Theoretical weight: 55.5 KDa
Source organism: Thermosphaera aggregans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9YGA8 (Residues: 1-481; Coverage: 100%)
Sequence domains: Glycosyl hydrolase family 1
Structure domains: Glycosidases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21212
Unit cell:
a: 117.509Å b: 102.215Å c: 95.776Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.21 0.249
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability.
Vieille et al. (2001)
4 more

4 mentions without citation

Structural basis for thermostability of beta-glycosidase from the thermophilic eubacterium Thermus nonproteolyticus HG102.
Wang et al. (2003)
3 more