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[[Image:1n8t.gif|left|200px]]<br /><applet load="1n8t" size="350" 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://oca.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://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:03:30 2008''

Latest revision as of 10:54, 14 February 2024

The crystal structure of phosphoglucose isomerase from rabbit muscleThe crystal structure of phosphoglucose isomerase from rabbit muscle

Structural highlights

1n8t is a 2 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1n8t, resolution 2.50Å

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