1n8t: Difference between revisions

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<StructureSection load='1n8t' size='340' side='right'caption='[[1n8t]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='1n8t' size='340' side='right'caption='[[1n8t]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1n8t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/European_rabbit European rabbit]. 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>
<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>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] </span></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]] 2.5&#8491;</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=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>
<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>
</table>
</table>
== Function ==
== Function ==
[[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).  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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].
</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].
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<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:12595702<ref>PMID:12595702</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1n8t" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Phosphoglucose isomerase 3D structures|Phosphoglucose isomerase 3D structures]]
*[[Phosphoglucose isomerase 3D structures|Phosphoglucose isomerase 3D structures]]
== References ==
<references/>
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__TOC__
</StructureSection>
</StructureSection>
[[Category: European rabbit]]
[[Category: Glucose-6-phosphate isomerase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Davies, C]]
[[Category: Oryctolagus cuniculus]]
[[Category: Muirhead, H]]
[[Category: Davies C]]
[[Category: Aldose-ketose isomerase]]
[[Category: Muirhead H]]
[[Category: Cytokine]]
[[Category: Glycolysis]]
[[Category: Isomerase]]