› 1spq

X-ray diffraction
2.16Å resolution

Understanding protein lids: Structural analysis of active hinge mutants in triosephosphate isomerase

Released:
DOI: 10.2210/pdb1spq/pdb
PDB entry 1spq coloured by chain, front view.
PDB entry 1spq coloured by chain, side view.
PDB entry 1spq coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase.
Kursula I, Salin M, Sun J, Norledge BV, Haapalainen AM, Sampson NS, Wierenga RK
Protein Eng Des Sel 17 375-82 (2004)
PMID: 15166315

Function and Biology Details

Reactions catalysed: 
Glycerone phosphate = methylglyoxal + phosphate
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-133701 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 247 amino acids
Theoretical weight: 26.58 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00940 (Residues: 2-248; Coverage: 100%)
Gene name: TPI1
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand PEG 3 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: C2
Unit cell:
a: 80.706Å b: 57.334Å c: 106.154Å
α: 90° β: 92.89° γ: 90°
R-values:
R R work R free
0.162 0.16 0.198
Expression system: Escherichia coli

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Citations

3 review citations

Triosephosphate isomerase: a highly evolved biocatalyst.
Wierenga et al. (2010)
2 more