› 2i9e

X-ray diffraction
2Å resolution

Structure of Triosephosphate Isomerase of Tenebrio molitor

Released:
DOI: 10.2210/pdb2i9e/pdb
PDB entry 2i9e coloured by chain, front view.
PDB entry 2i9e coloured by chain, side view.
PDB entry 2i9e coloured by chain, top view.
Source organism: Tenebrio molitor
Primary publication:
A coleopteran triosephosphate isomerase: X-ray structure and phylogenetic impact of insect sequences.
Knobeloch D, Schmidt A, Scheerer P, Krauss N, Wessner H, Scholz Ch, Küttner G, von Rintelen T, Wessel A, Höhne W
Insect Mol Biol 19 35-48 (2010)
PMID: 19849721

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185321 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 259 amino acids
Theoretical weight: 28.19 KDa
Source organism: Tenebrio molitor
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8MPF2 (Residues: 1-247; Coverage: 100%)
Gene names: GEV33_012778, tpi
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand TRS 5 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21
Unit cell:
a: 37.06Å b: 145.08Å c: 94.28Å
α: 90° β: 95.61° γ: 90°
R-values:
R R work R free
0.221 0.219 0.239
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Cellular and biochemical characterization of two closely related triosephosphate isomerases from Trichomonas vaginalis.
Figueroa-Angulo et al. (2012)
2 more

7 mentions without citation

A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication.
Dujardin et al. (2015)
6 more