2P3V
Thermotoga maritima IMPase TM1415
Summary for 2P3V
| Entry DOI | 10.2210/pdb2p3v/pdb |
| Related | 2P3N |
| Descriptor | Inositol-1-monophosphatase, S,R MESO-TARTARIC ACID (3 entities in total) |
| Functional Keywords | inositol, phosphatase, asymmetric tetramer, hydrolase |
| Biological source | Thermotoga maritima |
| Total number of polymer chains | 4 |
| Total formula weight | 115331.16 |
| Authors | Stieglitz, K.A.,Roberts, M.F.,Li, W.,Stec, B. (deposition date: 2007-03-09, release date: 2007-04-24, Last modification date: 2024-08-07) |
| Primary citation | Stieglitz, K.A.,Roberts, M.F.,Li, W.,Stec, B. Crystal structure of the tetrameric inositol 1-phosphate phosphatase (TM1415) from the hyperthermophile, Thermotoga maritima. Febs J., 274:2461-2469, 2007 Cited by PubMed Abstract: The structure of the first tetrameric inositol monophosphatase (IMPase) has been solved. This enzyme, from the eubacterium Thermotoga maritima, similarly to its archaeal homologs exhibits dual specificity with both IMPase and fructose-1,6-bisphosphatase activities. The tetrameric structure of this unregulated enzyme is similar, in its quaternary assembly, to the allosterically regulated tetramer of fructose-1,6-bisphosphatase. The individual dimers are similar to the human IMPase. Additionally, the structures of two crystal forms of IMPase show significant differences. In the first crystal form, the tetrameric structure is symmetrical, with the active site loop in each subunit folded into a beta-hairpin conformation. The second form is asymmetrical and shows an unusual structural change. Two of the subunits have the active site loop folded into a beta-hairpin structure, whereas in the remaining two subunits the same loop adopts an alpha-helical conformation. PubMed: 17419729DOI: 10.1111/j.0014-2956.2007.05779.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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