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PDBsum entry 2i9e

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protein ligands Protein-protein interface(s) links
Isomerase PDB id
2i9e
Jmol PyMol
Contents
Protein chains
246 a.a. *
Ligands
TRS ×5
Waters ×352
* Residue conservation analysis
PDB id:
2i9e
Name: Isomerase
Title: Structure of triosephosphate isomerase of tenebrio molitor
Structure: Triosephosphate isomerase. Chain: a, b, c, d. Engineered: yes. Mutation: yes
Source: Tenebrio molitor. Yellow mealworm. Organism_taxid: 7067. Gene: tpi. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
Resolution:
2.00Å     R-factor:   0.219     R-free:   0.239
Authors: A.Schmidt,P.Scheerer,H.Wessner,W.Hoehne,N.Krauss
Key ref: D.Knobeloch et al. (2010). A coleopteran triosephosphate isomerase: X-ray structure and phylogenetic impact of insect sequences. Insect Mol Biol, 19, 35-48. PubMed id: 19849721
Date:
05-Sep-06     Release date:   26-Sep-06    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8MPF2  (Q8MPF2_TENMO) -  Triosephosphate isomerase
Seq:
Struc:
247 a.a.
246 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.5.3.1.1  - Triose-phosphate isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: D-glyceraldehyde 3-phosphate = glycerone phosphate
D-glyceraldehyde 3-phosphate
= glycerone phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   4 terms 
  Biochemical function     catalytic activity     3 terms  

 

 
    Added reference    
 
 
Insect Mol Biol 19:35-48 (2010)
PubMed id: 19849721  
 
 
A coleopteran triosephosphate isomerase: X-ray structure and phylogenetic impact of insect sequences.
D.Knobeloch, A.Schmidt, P.Scheerer, N.Krauss, H.Wessner, C.h.Scholz, G.Küttner, T.von Rintelen, A.Wessel, W.Höhne.
 
  ABSTRACT  
 
A coleopteran triosephosphate isomerase (TIM) from Tenebrio molitor (yellow mealworm beetle) was recombinantly expressed in Escherichia coli and characterized with respect to thermal stability, kinetic parameters and oligomeric state. The enzyme was successfully crystallized and the structure determined by X-ray analysis to 2.0 A resolution. This is the first example of an invertebrate TIM. We compare structural features with known structures of TIMs from microorganisms, plants and vertebrates, and discuss the utility of the Tenebrio TIM sequence, together with several newly sequenced insect TIMs, for molecular phylogenetic analysis.
 

 

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