2p3v
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(New page: 200px<br /><applet load="2p3v" size="450" color="white" frame="true" align="right" spinBox="true" caption="2p3v, resolution 2.4Å" /> '''Thermotoga maritima I...)
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Revision as of 11:17, 21 November 2007
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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 SRT 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 Apr 10;. PMID:17419729
Page seeded by OCA on Wed Nov 21 13:24:52 2007
