2I9E

Structure of Triosephosphate Isomerase of Tenebrio molitor


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.239 
  • R-Value Work: 0.219 
  • R-Value Observed: 0.221 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

A coleopteran triosephosphate isomerase: X-ray structure and phylogenetic impact of insect sequences.

Knobeloch, D.Schmidt, A.Scheerer, P.Krauss, N.Wessner, H.Scholz, C.Kuttner, G.von Rintelen, T.Wessel, A.Hohne, W.

(2010) Insect Mol Biol 19: 35-48

  • DOI: https://doi.org/10.1111/j.1365-2583.2009.00928.x
  • Primary Citation of Related Structures:  
    2I9E

  • PubMed 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.


  • Organizational Affiliation

    Institut für Biochemie, Charité- Universitätsmedizin Berlin, Berlin.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Triosephosphate isomerase
A, B, C, D
259Tenebrio molitorMutation(s): 3 
Gene Names: tpi
EC: 5.3.1.1
UniProt
Find proteins for Q8MPF2 (Tenebrio molitor)
Explore Q8MPF2 
Go to UniProtKB:  Q8MPF2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8MPF2
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.239 
  • R-Value Work: 0.219 
  • R-Value Observed: 0.221 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 37.06α = 90
b = 145.08β = 95.61
c = 94.28γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
AMoREphasing
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-09-26
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2020-04-15
    Changes: Database references
  • Version 1.4: 2021-10-20
    Changes: Database references, Derived calculations
  • Version 1.5: 2023-08-30
    Changes: Data collection, Refinement description