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[[Image:1u0f.jpg|left|200px]]


{{Structure
==Crystal structure of mouse phosphoglucose isomerase in complex with glucose 6-phosphate==
|PDB= 1u0f |SIZE=350|CAPTION= <scene name='initialview01'>1u0f</scene>, resolution 1.60&Aring;
<StructureSection load='1u0f' size='340' side='right'caption='[[1u0f]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</scene>, <scene name='pdbligand=G6Q:GLUCOSE-6-PHOSPHATE'>G6Q</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
<table><tr><td colspan='2'>[[1u0f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U0F FirstGlance]. <br>
|ACTIVITY= [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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
|GENE= Gpi ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</scene>, <scene name='pdbligand=G6Q:GLUCOSE-6-PHOSPHATE'>G6Q</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1u0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u0f OCA], [https://pdbe.org/1u0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u0f RCSB], [https://www.ebi.ac.uk/pdbsum/1u0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u0f ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G6PI_MOUSE G6PI_MOUSE] 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.
== 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/u0/1u0f_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=1u0f ConSurf].
<div style="clear:both"></div>


'''Crystal structure of mouse phosphoglucose isomerase in complex with glucose 6-phosphate'''
==See Also==
 
*[[Phosphoglucose isomerase 3D structures|Phosphoglucose isomerase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Phosphoglucose isomerase (PGI) is an enzyme of glycolysis that interconverts glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P) but, outside the cell, is a multifunctional cytokine. High-resolution crystal structures of the enzyme from mouse have been determined in native form and in complex with the inhibitor erythrose 4-phosphate, and with the substrate glucose 6-phosphate. In the substrate-bound structure, the glucose sugar is observed in both straight-chain and ring forms. This structure supports a specific role for Lys518 in enzyme-catalyzed ring opening and we present a "push-pull" mechanism in which His388 breaks the O5-C1 bond by donating a proton to the ring oxygen atom and, simultaneously, Lys518 abstracts a proton from the C1 hydroxyl group. The reverse occurs in ring closure. The transition from ring form to straight-chain substrate is achieved through rotation of the C3-C4 bond, which brings the C1-C2 region into close proximity to Glu357, the base catalyst for the isomerization step. The structure with G6P also explains the specificity of PGI for glucose 6-phosphate over mannose 6-isomerase (M6P). To isomerize M6P to F6P requires a rotation of its C2-C3 bond but in PGI this is sterically blocked by Gln511.
[[Category: Large Structures]]
 
==About this Structure==
1U0F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U0F OCA].
 
==Reference==
The crystal structure of mouse phosphoglucose isomerase at 1.6A resolution and its complex with glucose 6-phosphate reveals the catalytic mechanism of sugar ring opening., Graham Solomons JT, Zimmerly EM, Burns S, Krishnamurthy N, Swan MK, Krings S, Muirhead H, Chirgwin J, Davies C, J Mol Biol. 2004 Sep 17;342(3):847-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15342241 15342241]
[[Category: Glucose-6-phosphate isomerase]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Burns S]]
[[Category: Burns, S.]]
[[Category: Chirgwin J]]
[[Category: Chirgwin, J.]]
[[Category: Davies C]]
[[Category: Davies, C.]]
[[Category: Krings S]]
[[Category: Krings, S.]]
[[Category: Krishnamurthy N]]
[[Category: Krishnamurthy, N.]]
[[Category: Muirhead H]]
[[Category: Muirhead, H.]]
[[Category: Solomons JTG]]
[[Category: Solomons, J T.G.]]
[[Category: Swan MK]]
[[Category: Swan, M K.]]
[[Category: Zimmerly EM]]
[[Category: Zimmerly, E M.]]
[[Category: BME]]
[[Category: G6P]]
[[Category: G6Q]]
[[Category: GOL]]
[[Category: SO4]]
[[Category: aldose-ketose isomerase]]
[[Category: dimer]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:25:39 2008''

Latest revision as of 11:43, 14 February 2024

Crystal structure of mouse phosphoglucose isomerase in complex with glucose 6-phosphateCrystal structure of mouse phosphoglucose isomerase in complex with glucose 6-phosphate

Structural highlights

1u0f is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

G6PI_MOUSE 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.

Evolutionary Conservation

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

See Also

1u0f, resolution 1.60Å

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