1n8t: Difference between revisions

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-[[Image:1n8t.gif|left|200px]]
- {{Structure
+==The crystal structure of phosphoglucose isomerase from rabbit muscle==
-|PDB= 1n8t |SIZE=350|CAPTION= <scene name='initialview01'>1n8t</scene>, resolution 2.50&Aring;
+<StructureSection load='1n8t' size='340' side='right'caption='[[1n8t]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<table><tr><td colspan='2'>[[1n8t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N8T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N8T FirstGlance]. <br>
-|ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
-|GENE=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1n8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n8t OCA], [https://pdbe.org/1n8t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n8t RCSB], [https://www.ebi.ac.uk/pdbsum/1n8t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n8t ProSAT]</span></td></tr>
-|DOMAIN=
+</table>
-|RELATEDENTRY=
+== Function ==
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n8t OCA], [http://www.ebi.ac.uk/pdbsum/1n8t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n8t RCSB]</span>
+[https://www.uniprot.org/uniprot/G6PI_RABIT G6PI_RABIT] 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 (By similarity).
-}}
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n8/1n8t_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1n8t ConSurf].
+<div style="clear:both"></div>
-'''The crystal structure of phosphoglucose isomerase from rabbit muscle'''
+==See Also==
+*[[Phosphoglucose isomerase 3D structures|Phosphoglucose isomerase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-Phosphoglucose isomerase (PGI) is a housekeeping enzyme of metabolism that catalyses the interconversion of glucose 6-phosphate and fructose 6-phosphate, with roles in the glycolytic and gluconeogenic pathways. PGI is also a multifunctional protein that manifests the properties of a cytokine in a wide array of cellular processes, including the production of immunoglobulin by B cells and tumour-cell differentiation. The crystal structure of PGI in the native form from rabbit muscle has been solved at a resolution of 2.5 A by a combination of multiple isomorphous replacement and multi-crystal averaging techniques. Comparison with published structures of rabbit PGI in complex with three inhibitors and with the substrate fructose 6-phosphate reveals a number of conformational changes that may be associated with catalytic function. These occur in the small domain around the sugar phosphate-binding site, in a small helix carrying His388 and in a helix near the C-terminal end. One of these may be the structural rearrangement that has been postulated to be the rate-limiting step for catalysis.
+[[Category: Large Structures]]
-==About this Structure==
-N8T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N8T OCA].
-==Reference==
-Structure of native phosphoglucose isomerase from rabbit: conformational changes associated with catalytic function., Davies C, Muirhead H, Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):453-65. Epub 2003, Feb 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12595702 12595702]
-[[Category: Glucose-6-phosphate isomerase]]
 [[Category: Oryctolagus cuniculus]]
-[[Category: Single protein]]
+[[Category: Davies C]]
-[[Category: Davies, C.]]
+[[Category: Muirhead H]]
-[[Category: Muirhead, H.]]
-[[Category: aldose-ketose isomerase]]
-[[Category: cytokine]]
-[[Category: glycolysis]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:26:58 2008''