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New page: left|200px<br /><applet load="1n8t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n8t, resolution 2.50Å" /> '''The crystal structur...
 
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[[Image:1n8t.gif|left|200px]]<br /><applet load="1n8t" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1n8t, resolution 2.50&Aring;" />
'''The crystal structure of phosphoglucose isomerase from rabbit muscle'''<br />


==Overview==
==The crystal structure of phosphoglucose isomerase from rabbit muscle==
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.
<StructureSection load='1n8t' size='340' side='right'caption='[[1n8t]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<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='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>
</table>
== 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).
== 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>


==About this Structure==
==See Also==
1N8T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N8T OCA].
*[[Phosphoglucose isomerase 3D structures|Phosphoglucose isomerase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12595702 12595702]
[[Category: Large Structures]]
[[Category: Glucose-6-phosphate isomerase]]
[[Category: Oryctolagus cuniculus]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:03:38 2007''

Latest revision as of 07:54, 14 February 2024

The crystal structure of phosphoglucose isomerase from rabbit muscle

1n8t, resolution 2.50Å

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