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1g0i

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Revision as of 06:17, 3 January 2018

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

Structural highlights

1g0i is a 2 chain structure with sequence from Atcc 43067. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1dk4, 1g0h
Activity:	Inositol-phosphate phosphatase, with EC number 3.1.3.25
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[BSUHB_METJA] Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P), 2'-AMP, pNPP, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate, fructose-6-phosphate, NAD(+) or 5'-AMP. May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate.^[1] ^[2]

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

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
↑ Chen L, Roberts MF. Cloning and expression of the inositol monophosphatase gene from Methanococcus jannaschii and characterization of the enzyme. Appl Environ Microbiol. 1998 Jul;64(7):2609-15. PMID:9647837
↑ Johnson KA, Chen L, Yang H, Roberts MF, Stec B. Crystal structure and catalytic mechanism of the MJ0109 gene product: a bifunctional enzyme with inositol monophosphatase and fructose 1,6-bisphosphatase activities. Biochemistry. 2001 Jan 23;40(3):618-30. PMID:11170378

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1g0i"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF MJ0109 GENE PRODUCT INOSITOL MONOPHOSPHATASE-FRUCTOSE 1,6 BISPHOSPHATASE==
 <StructureSection load='1g0i' size='340' side='right' caption='[[1g0i]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dk4|1dk4]], [[1g0h|1g0h]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0i OCA], [http://pdbe.org/1g0i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g0i RCSB], [http://www.ebi.ac.uk/pdbsum/1g0i PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0i OCA], [http://pdbe.org/1g0i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g0i RCSB], [http://www.ebi.ac.uk/pdbsum/1g0i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g0i ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g0/1g0i_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g0/1g0i_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1g0i" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Inositol Monophosphatase|Inositol Monophosphatase]]
 == References ==
 <references/>

1g0i

From Proteopedia

Revision as of 06:17, 3 January 2018

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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