Inositol Monophosphatase
From Proteopedia
(Difference between revisions)
(Introduction) |
|||
| Line 3: | Line 3: | ||
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | <!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
=Inositol Monophosphatase (1dk4)= | =Inositol Monophosphatase (1dk4)= | ||
| - | This protein structure is derived from the the methanogen ''Methanococcus jannaschii'' (MJ0109). Curiously this protein shows both Inositol Monophosphate (IMPase) activity as well as Fructose 1,6 Bisphosphatase acivity (FBPase)<ref>PMID: | + | Inositol Monophosphatse is a heteromdimeric phosphatase. This protein structure is derived from the the methanogen ''Methanococcus jannaschii'' (MJ0109). Curiously this protein shows both Inositol Monophosphate (IMPase) activity as well as Fructose 1,6 Bisphosphatase acivity (FBPase)<ref>PMID:11062561</ref>. This protein has a homolog in another archeabacteria, [[1lbv|''Archaeoglobus fulgidus'']]<ref>PMID:11940584</ref>. |
| - | {{STRUCTURE_1dk4|PDB=1dk4|SCENE=}} | + | {{STRUCTURE_1dk4|PDB=1dk4|SCENE=intro}} |
__TOC__ | __TOC__ | ||
| - | =''Methanococcus jannaschii'' | + | =''Methanococcus jannaschii''[http://en.wikipedia.org/wiki/Methanocaldococcus]= |
| - | + | :''M. jannaschii'' are thermophilc methane producing archeabacteria that were discovered in 1983 the manned submersible ALVIN<ref>DOI:10.1007/BF00425213</ref>. They were sampled from the base of a deep sea hydrothermal vent in 2600m of water, local tempurature was 85°C. The complete 1.66 mega base pairs of its genome has been sequenced, about 1738 genes were identified, most of them were determined to be homologous to eukaryotic proteins<ref>DOI:10.1126/science.273.5278.1058</ref>. | |
| - | + | =Structure= | |
| - | : | + | ''not sure what to include here'' |
| - | + | ==Ligand== | |
| - | + | :The active site requires 3 Zn and one Phosphate for acivity | |
| - | + | ||
| - | == | + | |
| - | + | ||
<scene name='Sandbox_Reserved_326/Blah/2'>reaction site</scene> | <scene name='Sandbox_Reserved_326/Blah/2'>reaction site</scene> | ||
| - | = | + | =Function= |
| + | Inositol monophosphatase activity signalling pathway, increases cytosolic Ca+² | ||
| + | ===bipolar disorder=== | ||
| + | descibe the disorder, and Li+ inhibition | ||
| + | FBPase gluconeogenesis, fructose 1,6 bisphosphate to fructose 6 phosphate. | ||
=References= | =References= | ||
<references/> | <references/> | ||
Revision as of 05:16, 19 March 2011
| This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada. |
To get started:
More help: Help:Editing |
Inositol Monophosphatase (1dk4)
Inositol Monophosphatse is a heteromdimeric phosphatase. This protein structure is derived from the the methanogen Methanococcus jannaschii (MJ0109). Curiously this protein shows both Inositol Monophosphate (IMPase) activity as well as Fructose 1,6 Bisphosphatase acivity (FBPase)[1]. This protein has a homolog in another archeabacteria, Archaeoglobus fulgidus[2]. Template:STRUCTURE 1dk4
Contents |
Methanococcus jannaschii[1]
- M. jannaschii are thermophilc methane producing archeabacteria that were discovered in 1983 the manned submersible ALVIN[3]. They were sampled from the base of a deep sea hydrothermal vent in 2600m of water, local tempurature was 85°C. The complete 1.66 mega base pairs of its genome has been sequenced, about 1738 genes were identified, most of them were determined to be homologous to eukaryotic proteins[4].
Structure
not sure what to include here
Ligand
- The active site requires 3 Zn and one Phosphate for acivity
Function
Inositol monophosphatase activity signalling pathway, increases cytosolic Ca+²
bipolar disorder
descibe the disorder, and Li+ inhibition FBPase gluconeogenesis, fructose 1,6 bisphosphate to fructose 6 phosphate.
References
- ↑ Stec B, Yang H, Johnson KA, Chen L, Roberts MF. MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase. Nat Struct Biol. 2000 Nov;7(11):1046-50. PMID:11062561 doi:10.1038/80968
- ↑ Stieglitz KA, Johnson KA, Yang H, Roberts MF, Seaton BA, Head JF, Stec B. Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop. J Biol Chem. 2002 Jun 21;277(25):22863-74. Epub 2002 Apr 8. PMID:11940584 doi:http://dx.doi.org/10.1074/jbc.M201042200
- ↑ doi: https://dx.doi.org/10.1007/BF00425213
- ↑ doi: https://dx.doi.org/10.1126/science.273.5278.1058
