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| | <StructureSection load='1b0z' size='340' side='right'caption='[[1b0z]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1b0z' size='340' side='right'caption='[[1b0z]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1b0z]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B0Z OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1B0Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1b0z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B0Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B0Z FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PGIB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b0z OCA], [https://pdbe.org/1b0z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b0z RCSB], [https://www.ebi.ac.uk/pdbsum/1b0z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b0z ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1b0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b0z OCA], [http://pdbe.org/1b0z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1b0z RCSB], [http://www.ebi.ac.uk/pdbsum/1b0z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1b0z ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/G6PI2_GEOSE G6PI2_GEOSE] Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.[HAMAP-Rule:MF_00473] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Phosphoglucoisomerase|Phosphoglucoisomerase]] | |
| | *[[Phosphoglucose isomerase 3D structures|Phosphoglucose isomerase 3D structures]] | | *[[Phosphoglucose isomerase 3D structures|Phosphoglucose isomerase 3D structures]] |
| | == References == | | == References == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 12980]] | + | [[Category: Geobacillus stearothermophilus]] |
| - | [[Category: Glucose-6-phosphate isomerase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, W S]] | + | [[Category: Chen W-S]] |
| - | [[Category: Chou, C C]] | + | [[Category: Chou C-C]] |
| - | [[Category: Hsiao, C D]] | + | [[Category: Hsiao C-D]] |
| - | [[Category: Meng, M]] | + | [[Category: Meng M]] |
| - | [[Category: Sun, Y J]] | + | [[Category: Sun Y-J]] |
| - | [[Category: Autocrinefactor]]
| + | |
| - | [[Category: Crystallography motility]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Neuroleukin]]
| + | |
| - | [[Category: Phosphoglucose isomerase]]
| + | |
| Structural highlights
Function
G6PI2_GEOSE Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.[HAMAP-Rule:MF_00473]
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
Phosphoglucose isomerase catalyzes the reversible isomerization of glucose 6-phosphate to fructose 6-phosphate. In addition, phosphoglucose isomerase has been shown to have functions equivalent to neuroleukin, autocrine motility factor, and maturation factor. Here we present the crystal structures of phosphoglucose isomerase complexed with 5-phospho-D-arabinonate and N-bromoacetylethanolamine phosphate at 2.5- and 2.3-A resolution, respectively. The inhibitors bind to a region within the domains' interface and interact with a histidine residue (His(306)) from the other subunit. We also demonstrated that the inhibitors not only affect the enzymatic activity of phosphoglucose isomerase, but can also inhibit the autocrine motility factor-induced cell motility of CT-26 mouse colon tumor cells. These results indicate that the substrate and the receptor binding sites of phosphoglucose isomerase and autocrine motility factor are located within close proximity to each other. Based on these two complex structures, together with biological and biochemical results, we propose a possible isomerization mechanism for phosphoglucose isomerase.
The crystal structure of phosphoglucose isomerase/autocrine motility factor/neuroleukin complexed with its carbohydrate phosphate inhibitors suggests its substrate/receptor recognition.,Chou CC, Sun YJ, Meng M, Hsiao CD J Biol Chem. 2000 Jul 28;275(30):23154-60. PMID:10770936[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chou CC, Sun YJ, Meng M, Hsiao CD. The crystal structure of phosphoglucose isomerase/autocrine motility factor/neuroleukin complexed with its carbohydrate phosphate inhibitors suggests its substrate/receptor recognition. J Biol Chem. 2000 Jul 28;275(30):23154-60. PMID:10770936 doi:10.1074/jbc.M002017200
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