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1dqr

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(New page: 200px<br /><applet load="1dqr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dqr, resolution 2.5&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1dqr.gif|left|200px]]<br /><applet load="1dqr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dqr, resolution 2.5&Aring;" />
 
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'''CRYSTAL STRUCTURE OF RABBIT PHOSPHOGLUCOSE ISOMERASE, A GLYCOLYTIC ENZYME THAT MOONLIGHTS AS NEUROLEUKIN, AUTOCRINE MOTILITY FACTOR, AND DIFFERENTIATION MEDIATOR'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF RABBIT PHOSPHOGLUCOSE ISOMERASE, A GLYCOLYTIC ENZYME THAT MOONLIGHTS AS NEUROLEUKIN, AUTOCRINE MOTILITY FACTOR, AND DIFFERENTIATION MEDIATOR==
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The multifunctional protein phosphoglucose isomerase, also known as, neuroleukin, autocrine motility factor, and differentiation and maturation, mediator, has different roles inside and outside the cell. In the, cytoplasm, it catalyzes the second step in glycolysis. Outside the cell, it serves as a nerve growth factor and cytokine. We have determined the, three-dimensional structure of rabbit muscle phosphoglucose isomerase, complexed with the competitive inhibitor D-gluconate 6-phosphate by X-ray, crystallography at 2.5 A resolution. The structure shows that the enzyme, is a dimer with two alpha/beta-sandwich domains in each subunit. The, location of the bound D-gluconate 6-phosphate inhibitor leads to the, identification of residues involved in substrate specificity (Ser209, Ser159, Thr214, Thr217, and Thr211). The results of previously published, kinetic studies suggest that a lysine and a histidine are involved in the, catalytic mechanism. The crystal structure suggests active site residues, Lys518 and His388 might be these residues. In addition, the positions of, amino acid residues that are substituted in the genetic disease, nonspherocytic hemolytic anemia suggest how these substitutions can result, in altered catalysis or protein stability.
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<StructureSection load='1dqr' size='340' side='right'caption='[[1dqr]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dqr]] 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=1DQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DQR FirstGlance]. <br>
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</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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6PG:6-PHOSPHOGLUCONIC+ACID'>6PG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dqr OCA], [https://pdbe.org/1dqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dqr RCSB], [https://www.ebi.ac.uk/pdbsum/1dqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dqr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dq/1dqr_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1dqr ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1DQR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with 6PG as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1DQR OCA].
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*[[Phosphoglucose isomerase 3D structures|Phosphoglucose isomerase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of rabbit phosphoglucose isomerase, a glycolytic enzyme that moonlights as neuroleukin, autocrine motility factor, and differentiation mediator., Jeffery CJ, Bahnson BJ, Chien W, Ringe D, Petsko GA, Biochemistry. 2000 Feb 8;39(5):955-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10653639 10653639]
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[[Category: Large Structures]]
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[[Category: Glucose-6-phosphate isomerase]]
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[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Single protein]]
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[[Category: Bahnson BJ]]
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[[Category: Bahnson, B.J.]]
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[[Category: Jeffery CJ]]
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[[Category: Jeffery, C.J.]]
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[[Category: Petsko GA]]
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[[Category: Petsko, G.A.]]
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[[Category: Ringe D]]
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[[Category: Ringe, D.]]
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[[Category: 6PG]]
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[[Category: alpha-beta sandwich domains]]
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[[Category: anti-parallel beta sheet]]
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[[Category: parallel beta sheet]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:30:07 2007''
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Current revision

CRYSTAL STRUCTURE OF RABBIT PHOSPHOGLUCOSE ISOMERASE, A GLYCOLYTIC ENZYME THAT MOONLIGHTS AS NEUROLEUKIN, AUTOCRINE MOTILITY FACTOR, AND DIFFERENTIATION MEDIATOR

PDB ID 1dqr

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