1nuh

From Proteopedia

(Difference between revisions)

Current revision

The crystal structure of human phosphoglucose isomerase complexed with 5-phosphoarabinonate

Structural highlights

1nuh is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.51Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

Categories: Homo sapiens | Large Structures | Davies C

@@ Line 3: / Line 3: @@
 <StructureSection load='1nuh' size='340' side='right'caption='[[1nuh]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
 == 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]] 2.51&#8491;</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>
 == 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 ==
-[[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 19: / Line 17: @@
   <jmolCheckbox>
     <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/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 35: / Line 33: @@
 ==See Also==
-*[[Phosphoglucoisomerase|Phosphoglucoisomerase]]
 *[[Phosphoglucose isomerase 3D structures|Phosphoglucose isomerase 3D structures]]
 == References ==
@@ Line 41: / Line 38: @@
 __TOC__
 </StructureSection>
-[[Category: Glucose-6-phosphate isomerase]]
+[[Category: Homo sapiens]]
-[[Category: Human]]
 [[Category: Large Structures]]
-[[Category: Davies, C]]
+[[Category: Davies C]]
-[[Category: Aldose-ketose isomerase]]
-[[Category: Cytokine]]
-[[Category: Glycolysis enzyme]]
-[[Category: Isomerase]]
-[[Category: Neurotrophic growth factor]]

1nuh

From Proteopedia

Current revision

The crystal structure of human phosphoglucose isomerase complexed with 5-phosphoarabinonate

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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