1umg

From Proteopedia

(Difference between revisions)

Revision as of 14:25, 22 December 2016

Crystal structure of fructose-1,6-bisphosphatase

Structural highlights

1umg is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Activity:	Fructose-bisphosphatase, with EC number 3.1.3.11
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

As the first structure of the novel class of fructose-1,6-bisphosphatase (FBPase) present in thermophilic archaea, we solved the crystal structure of the ST0318 gene product (St-Fbp) of Sulfolobus tokodaii strain 7. The St-Fbp structure comprises a homooctamer of the 422 point-group. The protein folds as a four-layer alpha-beta-beta-alpha sandwich with a novel topology, which is completely different from the sugar phosphatase fold. The structure contains an unhydrolyzed FBP molecule in the open-keto form, as well as four hexacoordinated magnesium ions around the 1-phosphoryl group of FBP. The arrangement of the catalytic side chains and metal ligands is consistent with the three-metal ion assisted catalysis proposed for conventional FBPases. The structure provides an insight into the structural basis of the strict substrate specificity of St-Fbp.

The first crystal structure of the novel class of fructose-1,6-bisphosphatase present in thermophilic archaea.,Nishimasu H, Fushinobu S, Shoun H, Wakagi T Structure. 2004 Jun;12(6):949-59. PMID:15274916^[1]

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

References

↑ Nishimasu H, Fushinobu S, Shoun H, Wakagi T. The first crystal structure of the novel class of fructose-1,6-bisphosphatase present in thermophilic archaea. Structure. 2004 Jun;12(6):949-59. PMID:15274916 doi:10.1016/j.str.2004.03.026

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
-==Crystal strucure of fructose-1,6-bisphosphatase==
+==Crystal structure of fructose-1,6-bisphosphatase==
 <StructureSection load='1umg' size='340' side='right' caption='[[1umg]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1umg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulto Sulto]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UMG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UMG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1umg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UMG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UMG FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2FP:1,6-FRUCTOSE+DIPHOSPHATE+(LINEAR+FORM)'>2FP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ST0318 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273063 SULTO])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11] </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=1umg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1umg OCA], [http://pdbe.org/1umg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1umg RCSB], [http://www.ebi.ac.uk/pdbsum/1umg 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=1umg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1umg OCA], [http://pdbe.org/1umg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1umg RCSB], [http://www.ebi.ac.uk/pdbsum/1umg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1umg ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 35: / Line 35: @@
 </StructureSection>
 [[Category: Fructose-bisphosphatase]]
-[[Category: Sulto]]
 [[Category: Fushinobu, S]]
 [[Category: Nishimasu, H]]

1umg

From Proteopedia

Revision as of 14:25, 22 December 2016

Crystal structure of fructose-1,6-bisphosphatase

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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