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| | <StructureSection load='1nuh' size='340' side='right'caption='[[1nuh]], [[Resolution|resolution]] 2.51Å' scene=''> | | <StructureSection load='1nuh' size='340' side='right'caption='[[1nuh]], [[Resolution|resolution]] 2.51Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1nuh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NUH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1NUH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1nuh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NUH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NUH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PA5:5-PHOSPHOARABINONIC+ACID'>PA5</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.51Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1iat|1iat]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PA5:5-PHOSPHOARABINONIC+ACID'>PA5</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GPI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1nuh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nuh OCA], [https://pdbe.org/1nuh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nuh RCSB], [https://www.ebi.ac.uk/pdbsum/1nuh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nuh ProSAT]</span></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'>[http://proteopedia.org/fgij/fg.htm?mol=1nuh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nuh OCA], [http://pdbe.org/1nuh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nuh RCSB], [http://www.ebi.ac.uk/pdbsum/1nuh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nuh ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN]] Defects in GPI are the cause of hemolytic anemia non-spherocytic due to glucose phosphate isomerase deficiency (HA-GPID) [MIM:[http://omim.org/entry/613470 613470]]. It is a form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency. Severe GPI deficiency can be associated with hydrops fetalis, immediate neonatal death and neurological impairment. | + | [https://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN] Defects in GPI are the cause of hemolytic anemia non-spherocytic due to glucose phosphate isomerase deficiency (HA-GPID) [MIM:[https://omim.org/entry/613470 613470]. It is a form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency. Severe GPI deficiency can be associated with hydrops fetalis, immediate neonatal death and neurological impairment. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN]] Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons.<ref>PMID:11004567</ref> <ref>PMID:11437381</ref> <ref>PMID:12163179</ref> | + | [https://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN] Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons.<ref>PMID:11004567</ref> <ref>PMID:11437381</ref> <ref>PMID:12163179</ref> |
| | == 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: Glucose-6-phosphate isomerase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Davies, C]] | + | [[Category: Davies C]] |
| - | [[Category: Aldose-ketose isomerase]]
| + | |
| - | [[Category: Cytokine]]
| + | |
| - | [[Category: Glycolysis enzyme]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Neurotrophic growth factor]]
| + | |
| Structural highlights
Disease
G6PI_HUMAN Defects in GPI are the cause of hemolytic anemia non-spherocytic due to glucose phosphate isomerase deficiency (HA-GPID) [MIM:613470. It is a form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency. Severe GPI deficiency can be associated with hydrops fetalis, immediate neonatal death and neurological impairment.
Function
G6PI_HUMAN Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons.[1] [2] [3]
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 (PGI) is a workhorse enzyme of carbohydrate metabolism that interconverts glucose 6-phosphate and fructose 6-phosphate. Outside the cell, however, the protein appears to function as a cytokine. A crystal structure of human PGI bound with 5-phosphoarabinonate, a strong inhibitor that mimics the cis-enediol(ate) intermediate of the reaction, has been determined at 2.5 A resolution. The structure helps to confirm the assignment of Glu357 as the base catalyst in the isomerase reaction.
The structure of human phosphoglucose isomerase complexed with a transition-state analogue.,Davies C, Muirhead H, Chirgwin J Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):1111-3. Epub 2003, May 23. PMID:12777791[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Haga A, Niinaka Y, Raz A. Phosphohexose isomerase/autocrine motility factor/neuroleukin/maturation factor is a multifunctional phosphoprotein. Biochim Biophys Acta. 2000 Jul 14;1480(1-2):235-44. PMID:11004567
- ↑ Funasaka T, Haga A, Raz A, Nagase H. Tumor autocrine motility factor is an angiogenic factor that stimulates endothelial cell motility. Biochem Biophys Res Commun. 2001 Jul 6;285(1):118-28. PMID:11437381 doi:10.1006/bbrc.2001.5135
- ↑ Amraei M, Nabi IR. Species specificity of the cytokine function of phosphoglucose isomerase. FEBS Lett. 2002 Aug 14;525(1-3):151-5. PMID:12163179
- ↑ Davies C, Muirhead H, Chirgwin J. The structure of human phosphoglucose isomerase complexed with a transition-state analogue. Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):1111-3. Epub 2003, May 23. PMID:12777791
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