2p3v

From Proteopedia

(Difference between revisions)

Revision as of 23:21, 11 September 2015

Thermotoga maritima IMPase TM1415

Structural highlights

2p3v is a 4 chain structure with sequence from Thema. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2p3n
Gene:	suhB (THEMA)
Activity:	Inositol-phosphate phosphatase, with EC number 3.1.3.25
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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.^[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

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^[3]

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

References

↑ Chen L, Roberts MF. Characterization of a tetrameric inositol monophosphatase from the hyperthermophilic bacterium Thermotoga maritima. Appl Environ Microbiol. 1999 Oct;65(10):4559-67. PMID:10508089
↑ 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, Roberts MF, Li W, Stec B. Crystal structure of the tetrameric inositol 1-phosphate phosphatase (TM1415) from the hyperthermophile, Thermotoga maritima. FEBS J. 2007 May;274(10):2461-9. Epub 2007 Apr 10. PMID:17419729 doi:http://dx.doi.org/10.1111/j.0014-2956.2007.05779.x

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2p3v"

@@ Line 2: / Line 2: @@
 <StructureSection load='2p3v' size='340' side='right' caption='[[2p3v]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2p3v]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P3V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2P3V FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2p3v]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P3V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2P3V FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SRT:S,R+MESO-TARTARIC+ACID'>SRT</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2p3n|2p3n]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">suhB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">suhB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</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=2p3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p3v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2p3v RCSB], [http://www.ebi.ac.uk/pdbsum/2p3v 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=2p3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p3v OCA], [http://pdbe.org/2p3v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2p3v RCSB], [http://www.ebi.ac.uk/pdbsum/2p3v PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SUHB_THEMA SUHB_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.<ref>PMID:10508089</ref> <ref>PMID:11062561</ref>
+[[http://www.uniprot.org/uniprot/BSUHB_THEMA 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.<ref>PMID:10508089</ref> <ref>PMID:11062561</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 29: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2p3v" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 37: / Line 38: @@
 </StructureSection>
 [[Category: Inositol-phosphate phosphatase]]
-[[Category: Thermotoga maritima]]
+[[Category: Thema]]
 [[Category: Li, W]]
 [[Category: Roberts, M F]]

2p3v

From Proteopedia

Revision as of 23:21, 11 September 2015

Thermotoga maritima IMPase TM1415

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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