2I9E
Structure of Triosephosphate Isomerase of Tenebrio molitor
Summary for 2I9E
| Entry DOI | 10.2210/pdb2i9e/pdb |
| Descriptor | Triosephosphate isomerase, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total) |
| Functional Keywords | triosephosphate isomerase tenebrio molitor, isomerase |
| Biological source | Tenebrio molitor (yellow mealworm) |
| Total number of polymer chains | 4 |
| Total formula weight | 113379.62 |
| Authors | Schmidt, A.,Scheerer, P.,Wessner, H.,Hoehne, W.,Krauss, N. (deposition date: 2006-09-05, release date: 2006-09-26, Last modification date: 2023-08-30) |
| Primary citation | Knobeloch, D.,Schmidt, A.,Scheerer, P.,Krauss, N.,Wessner, H.,Scholz, C.,Kuttner, G.,von Rintelen, T.,Wessel, A.,Hohne, W. A coleopteran triosephosphate isomerase: X-ray structure and phylogenetic impact of insect sequences. Insect Mol Biol, 19:35-48, 2010 Cited by 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. PubMed: 19849721DOI: 10.1111/j.1365-2583.2009.00928.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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