› 2btm

X-ray diffraction
2.4Å resolution

DOES THE HIS12-LYS13 PAIR PLAY A ROLE IN THE ADAPTATION OF THERMOPHILIC TIMS TO HIGH TEMPERATURES?

Released:
DOI: 10.2210/pdb2btm/pdb
PDB entry 2btm coloured by chain, front view.
PDB entry 2btm coloured by chain, side view.
PDB entry 2btm coloured by chain, top view.
Source organism: Geobacillus stearothermophilus
Primary publication:
Lys13 plays a crucial role in the functional adaptation of the thermophilic triose-phosphate isomerase from Bacillus stearothermophilus to high temperatures.
Alvarez M, Wouters J, Maes D, Mainfroid V, Rentier-Delrue F, Wyns L, Depiereux E, Martial JA
J Biol Chem 274 19181-7 (1999)
PMID: 10383424

Function and Biology Details

Reaction catalysed: 
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133704 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 252 amino acids
Theoretical weight: 26.98 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00943 (Residues: 2-253; Coverage: 100%)
Gene names: tpi, tpiA
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand PGA 2 x PGA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.5
Spacegroup: P21212
Unit cell:
a: 78.132Å b: 107.913Å c: 70.98Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 0.22
Expression system: Escherichia coli

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Citations

2 review citations

Review: Protein function at thermal extremes: balancing stability and flexibility.
Fields PA. (2001)
1 more

4 mentions without citation

The Blueprint of a Minimal Cell: MiniBacillus.
Reuß et al. (2016)
3 more