2p3v
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The structure of the first tetrameric inositol monophosphatase (IMPase) | + | 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. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Crystal structure of the tetrameric inositol 1-phosphate phosphatase (TM1415) from the hyperthermophile, Thermotoga maritima., Stieglitz KA, Roberts MF, Li W, Stec B, FEBS J. 2007 Apr 10 | + | Crystal structure of the tetrameric inositol 1-phosphate phosphatase (TM1415) from the hyperthermophile, Thermotoga maritima., Stieglitz KA, Roberts MF, Li W, Stec B, FEBS J. 2007 May;274(10):2461-9. Epub 2007 Apr 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17419729 17419729] |
[[Category: Inositol-phosphate phosphatase]] | [[Category: Inositol-phosphate phosphatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
[[Category: Li, W.]] | [[Category: Li, W.]] | ||
| - | [[Category: Roberts, M | + | [[Category: Roberts, M F.]] |
[[Category: Stec, B.]] | [[Category: Stec, B.]] | ||
| - | [[Category: Stieglitz, K | + | [[Category: Stieglitz, K A.]] |
[[Category: SRT]] | [[Category: SRT]] | ||
[[Category: asymmetric tetramer]] | [[Category: asymmetric tetramer]] | ||
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[[Category: phosphatase]] | [[Category: phosphatase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:25:38 2008'' |
Revision as of 16:25, 21 February 2008
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Thermotoga maritima IMPase TM1415
Overview
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.
About this Structure
2P3V is a Single protein structure of sequence from Thermotoga maritima with as ligand. Active as Inositol-phosphate phosphatase, with EC number 3.1.3.25 Full crystallographic information is available from OCA.
Reference
Crystal structure of the tetrameric inositol 1-phosphate phosphatase (TM1415) from the hyperthermophile, Thermotoga maritima., Stieglitz KA, Roberts MF, Li W, Stec B, FEBS J. 2007 May;274(10):2461-9. Epub 2007 Apr 10. PMID:17419729
Page seeded by OCA on Thu Feb 21 18:25:38 2008
