1koj

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[[Image:1koj.gif|left|200px]]
 
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{{Structure
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==Crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonohydroxamic acid==
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|PDB= 1koj |SIZE=350|CAPTION= <scene name='initialview01'>1koj</scene>, resolution 1.90&Aring;
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<StructureSection load='1koj' size='340' side='right'caption='[[1koj]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=PAN:5-PHOSPHO-D-ARABINOHYDROXAMIC+ACID'>PAN</scene>
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<table><tr><td colspan='2'>[[1koj]] 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=1KOJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KOJ FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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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]] 1.9&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PAN:5-PHOSPHO-D-ARABINOHYDROXAMIC+ACID'>PAN</scene></td></tr>
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|DOMAIN=
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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=1koj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1koj OCA], [https://pdbe.org/1koj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1koj RCSB], [https://www.ebi.ac.uk/pdbsum/1koj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1koj ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1dqr|1DQR]], [[1hox|1HOX]], [[1hm5|1HM5]], [[1iat|1IAT]], [[1g98|1G98]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1koj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1koj OCA], [http://www.ebi.ac.uk/pdbsum/1koj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1koj RCSB]</span>
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== Function ==
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}}
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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/ko/1koj_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=1koj ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Phosphoglucose isomerase (EC ) catalyzes the second step in glycolysis, the reversible isomerization of D-glucose 6-phosphate to D-fructose 6-phosphate. The reaction mechanism involves acid-base catalysis with proton transfer and proceeds through a cis-enediol(ate) intermediate. 5-Phospho-D-arabinonohydroxamic acid (5PAH) is a synthetic small molecule that resembles the reaction intermediate, differing only in that it has a nitrogen atom in place of C1. Hence, 5PAH is the best inhibitor of the isomerization reaction reported to date with a K(i) of 2 x 10(-7) M. Here we report the crystal structure of rabbit phosphoglucose isomerase complexed with 5PAH at 1.9 A resolution. The interaction of 5PAH with amino acid residues in the enzyme active site supports a model of the catalytic mechanism in which Glu-357 transfers a proton between C1 and C2 and Arg-272 helps stabilize the intermediate. It also suggests a mechanism for proton transfer between O1 and O2.
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'''Crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonohydroxamic acid'''
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The crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonohydroxamic acid.,Arsenieva D, Hardre R, Salmon L, Jeffery CJ Proc Natl Acad Sci U S A. 2002 Apr 30;99(9):5872-7. PMID:11983887<ref>PMID:11983887</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1koj" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Phosphoglucose isomerase (EC ) catalyzes the second step in glycolysis, the reversible isomerization of D-glucose 6-phosphate to D-fructose 6-phosphate. The reaction mechanism involves acid-base catalysis with proton transfer and proceeds through a cis-enediol(ate) intermediate. 5-Phospho-D-arabinonohydroxamic acid (5PAH) is a synthetic small molecule that resembles the reaction intermediate, differing only in that it has a nitrogen atom in place of C1. Hence, 5PAH is the best inhibitor of the isomerization reaction reported to date with a K(i) of 2 x 10(-7) M. Here we report the crystal structure of rabbit phosphoglucose isomerase complexed with 5PAH at 1.9 A resolution. The interaction of 5PAH with amino acid residues in the enzyme active site supports a model of the catalytic mechanism in which Glu-357 transfers a proton between C1 and C2 and Arg-272 helps stabilize the intermediate. It also suggests a mechanism for proton transfer between O1 and O2.
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*[[Phosphoglucose isomerase 3D structures|Phosphoglucose isomerase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1KOJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KOJ OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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The crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonohydroxamic acid., Arsenieva D, Hardre R, Salmon L, Jeffery CJ, Proc Natl Acad Sci U S A. 2002 Apr 30;99(9):5872-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11983887 11983887]
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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: Arsenieva D]]
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[[Category: Arsenieva, D.]]
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[[Category: Hardre R]]
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[[Category: Hardre, R.]]
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[[Category: Jeffery CJ]]
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[[Category: Jeffery, C J.]]
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[[Category: Salmon L]]
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[[Category: Salmon, L.]]
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[[Category: protein - inhibitor complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:51:25 2008''
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Current revision

Crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonohydroxamic acid

PDB ID 1koj

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