2p3v

Thermotoga maritima IMPase TM1415

spinqualitylabelsall models 2p3v, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2p3v is a 4 chain structure with sequence from Thermotoga maritima MSB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: SRT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BSUHB_THEMA Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P) but displaying a 20-fold higher rate of hydrolysis of D-I-1-P than of the L isomer, 2'-AMP, pNPP, inositol-2-phosphate, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate, fructose-6-phosphate, 5'-AMP and NAD(+). May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Inositol monophosphatase 3D structures

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