Inositol Monophosphatase: Difference between revisions
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=Inositol Monophosphatase (1DK4)= | =Inositol Monophosphatase (1DK4)= | ||
Inositol Monophosphatase is a homodimeric phosphatase. This protein structure is derived from the the methanogen ''Methanococcus jannaschii'' gene MJ0109. Curiously this protein shows both Inositol Monophosphate (IMPase) activity as well as Fructose 1,6 Bisphosphatase acivity (FBPase)<ref name="rasmol">PMID:11062561</ref>. This protein has a homolog in another archeabacteria, [[1lbv|''Archaeoglobus fulgidus'']]<ref>PMID:11940584</ref>. It is thought to be a precursor of many phophatases in higher organisms<ref name="rasmol"/>. | |||
{{STRUCTURE_1dk4|PDB=1dk4|SCENE=}} | {{STRUCTURE_1dk4|PDB=1dk4|SCENE=Sandbox_Reserved_326/Begining/1}} | ||
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=''Methanococcus jannaschii''[http://en.wikipedia.org/wiki/Methanocaldococcus]= | =''Methanococcus jannaschii''[http://en.wikipedia.org/wiki/Methanocaldococcus]= | ||
''M. jannaschii'' are thermophilc methane producing archeabacteria that were discovered in 1983 the manned submersible ALVIN[http://www.springerlink.com/content/u8774k126821777x/]. 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>PMID: 8688087</ref>. | ''M. jannaschii'' are thermophilc methane producing archeabacteria that were discovered in 1983 the manned submersible ALVIN[http://www.springerlink.com/content/u8774k126821777x/]. 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>PMID: 8688087</ref>. | ||
=Structure= | =Structure= | ||
The general structure of this enzyme is a homodimer, composed of 253 amino acid residues. IMPase falls within the metallo-phosphatase family<ref | The general structure of this enzyme is a homodimer, composed of 253 amino acid residues. IMPase falls within the metallo-phosphatase family<ref name="rasmol"/>. This particular structure has been crystalized in complex with a <scene name='Sandbox_Reserved_326/Ligands/2'>phosphate group</scene> (<font color='red'>Red</font> and <font color='orange'>orange</font>), and three inhibitory Zn2+ ions (<font color='grey'>grey</font>) per subunit. Each subunit is composed of <scene name='Sandbox_Reserved_326/2nd_structure/1'>5 layers</scene> alternating helix, sheet, helix, sheet, then helix. Additionally, each subunit possess its own large hydrophilic active site. | ||
=Function= | =Function= | ||
IMPase activity within ''M. jannaschii'' is mainly limited to the production of a unique inositol, di-''myo''-inositol-1,1'-phosphate (DIP). Intracellular DIP concentrations increase usually in response to supraoptimal growth temperatures, and is involved in maintaining high cellular concentration of K+ which sustains optimal enzyme activity<ref>PMID: 9683472</ref>. | IMPase activity within ''M. jannaschii'' is mainly limited to the production of a unique inositol, di-''myo''-inositol-1,1'-phosphate (DIP). Intracellular DIP concentrations increase usually in response to supraoptimal growth temperatures, and is involved in maintaining high cellular concentration of K+ which sustains optimal enzyme activity<ref>PMID: 9683472</ref>. | ||
