1g0h

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[[Image:1g0h.jpg|left|200px]]
[[Image:1g0h.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1g0h |SIZE=350|CAPTION= <scene name='initialview01'>1g0h</scene>, resolution 2.3&Aring;
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The line below this paragraph, containing "STRUCTURE_1g0h", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=IPD:D-MYO-INOSITOL-1-PHOSPHATE'>IPD</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Inositol-phosphate_phosphatase Inositol-phosphate phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.25 3.1.3.25] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1g0h| PDB=1g0h | SCENE= }}
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|RELATEDENTRY=[[1dk4|1DK4]], [[1g0i|1G0I]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0h OCA], [http://www.ebi.ac.uk/pdbsum/1g0h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g0h RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF MJ0109 GENE PRODUCT INOSITOL MONOPHOSPHATASE-FRUCTOSE 1,6 BISPHOSPHATASE'''
'''CRYSTAL STRUCTURE OF MJ0109 GENE PRODUCT INOSITOL MONOPHOSPHATASE-FRUCTOSE 1,6 BISPHOSPHATASE'''
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[[Category: Stec, B.]]
[[Category: Stec, B.]]
[[Category: Yang, H.]]
[[Category: Yang, H.]]
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[[Category: complexed with ca2+ and i-1-p]]
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[[Category: Complexed with ca2+ and i-1-p]]
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[[Category: homodimer]]
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[[Category: Homodimer]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:58:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:33:55 2008''
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Revision as of 13:58, 2 May 2008

Image:1g0h.jpg

Template:STRUCTURE 1g0h

CRYSTAL STRUCTURE OF MJ0109 GENE PRODUCT INOSITOL MONOPHOSPHATASE-FRUCTOSE 1,6 BISPHOSPHATASE


Overview

Inositol monophosphatase (EC 3.1.3.25) in hyperthermophilic archaea is thought to play a role in the biosynthesis of di-myo-inositol-1,1'-phosphate (DIP), an osmolyte unique to hyperthermophiles. The Methanococcus jannaschii MJ109 gene product, the sequence of which is substantially homologous to that of human inositol monophosphatase, exhibits inositol monophosphatase activity but with substrate specificity that is broader than those of bacterial and eukaryotic inositol monophosphatases (it can also act as a fructose bisphosphatase). To understand its substrate specificity as well as the poor inhibition by Li(+) (a potent inhibitor of the mammalian enzyme), we have crystallized the enzyme and determined its three-dimensional structure. The overall fold, as expected, is similar to that of the mammalian enzyme, but the details suggest a closer relationship to fructose 1,6-bisphosphatases. Three complexes of the MJ0109 protein with substrate and/or product and inhibitory as well as activating metal ions suggest that the phosphatase mechanism is a three-metal ion assisted catalysis which is in variance with that proposed previously for the human inositol monophosphatase.

About this Structure

1G0H is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.

Reference

Crystal structure and catalytic mechanism of the MJ0109 gene product: a bifunctional enzyme with inositol monophosphatase and fructose 1,6-bisphosphatase activities., Johnson KA, Chen L, Yang H, Roberts MF, Stec B, Biochemistry. 2001 Jan 23;40(3):618-30. PMID:11170378 Page seeded by OCA on Fri May 2 16:58:39 2008

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