1nuh: Difference between revisions
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==The crystal structure of human phosphoglucose isomerase complexed with 5-phosphoarabinonate== | ==The crystal structure of human phosphoglucose isomerase complexed with 5-phosphoarabinonate== | ||
<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=''> | ||
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<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='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='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='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://oca.weizmann.ac.il/oca-docs/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]</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=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 == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nu/1nuh_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nu/1nuh_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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==See Also== | ==See Also== | ||
*[[Phosphoglucoisomerase|Phosphoglucoisomerase]] | *[[Phosphoglucoisomerase|Phosphoglucoisomerase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 21:39, 24 January 2018
The crystal structure of human phosphoglucose isomerase complexed with 5-phosphoarabinonateThe crystal structure of human phosphoglucose isomerase complexed with 5-phosphoarabinonate
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 PubMedPhosphoglucose 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 AlsoReferences
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