1b0z

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[[Image:1b0z.gif|left|200px]]
 
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{{Structure
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==The crystal structure of phosphoglucose isomerase-an enzyme with autocrine motility factor activity in tumor cells==
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|PDB= 1b0z |SIZE=350|CAPTION= <scene name='initialview01'>1b0z</scene>, resolution 2.3&Aring;
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<StructureSection load='1b0z' size='340' side='right'caption='[[1b0z]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1b0z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B0Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B0Z 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]] 2.3&#8491;</td></tr>
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|GENE= PGIB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 Geobacillus stearothermophilus])
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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=1b0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b0z OCA], [https://pdbe.org/1b0z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b0z RCSB], [https://www.ebi.ac.uk/pdbsum/1b0z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b0z ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b0z OCA], [http://www.ebi.ac.uk/pdbsum/1b0z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b0z RCSB]</span>
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[https://www.uniprot.org/uniprot/G6PI2_GEOSE G6PI2_GEOSE] Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.[HAMAP-Rule:MF_00473]
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}}
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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/b0/1b0z_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=1b0z 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 catalyzes the reversible isomerization of glucose 6-phosphate to fructose 6-phosphate. In addition, phosphoglucose isomerase has been shown to have functions equivalent to neuroleukin, autocrine motility factor, and maturation factor. Here we present the crystal structures of phosphoglucose isomerase complexed with 5-phospho-D-arabinonate and N-bromoacetylethanolamine phosphate at 2.5- and 2.3-A resolution, respectively. The inhibitors bind to a region within the domains' interface and interact with a histidine residue (His(306)) from the other subunit. We also demonstrated that the inhibitors not only affect the enzymatic activity of phosphoglucose isomerase, but can also inhibit the autocrine motility factor-induced cell motility of CT-26 mouse colon tumor cells. These results indicate that the substrate and the receptor binding sites of phosphoglucose isomerase and autocrine motility factor are located within close proximity to each other. Based on these two complex structures, together with biological and biochemical results, we propose a possible isomerization mechanism for phosphoglucose isomerase.
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'''The crystal structure of phosphoglucose isomerase-an enzyme with autocrine motility factor activity in tumor cells'''
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The crystal structure of phosphoglucose isomerase/autocrine motility factor/neuroleukin complexed with its carbohydrate phosphate inhibitors suggests its substrate/receptor recognition.,Chou CC, Sun YJ, Meng M, Hsiao CD J Biol Chem. 2000 Jul 28;275(30):23154-60. PMID:10770936<ref>PMID:10770936</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 1b0z" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Phosphoglucose isomerase catalyzes the reversible isomerization of glucose 6-phosphate to fructose 6-phosphate. In addition, phosphoglucose isomerase has been shown to have functions equivalent to neuroleukin, autocrine motility factor, and maturation factor. Here we present the crystal structures of phosphoglucose isomerase complexed with 5-phospho-D-arabinonate and N-bromoacetylethanolamine phosphate at 2.5- and 2.3-A resolution, respectively. The inhibitors bind to a region within the domains' interface and interact with a histidine residue (His(306)) from the other subunit. We also demonstrated that the inhibitors not only affect the enzymatic activity of phosphoglucose isomerase, but can also inhibit the autocrine motility factor-induced cell motility of CT-26 mouse colon tumor cells. These results indicate that the substrate and the receptor binding sites of phosphoglucose isomerase and autocrine motility factor are located within close proximity to each other. Based on these two complex structures, together with biological and biochemical results, we propose a possible isomerization mechanism for phosphoglucose isomerase.
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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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1B0Z is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B0Z OCA].
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__TOC__
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</StructureSection>
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==Reference==
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The crystal structure of phosphoglucose isomerase/autocrine motility factor/neuroleukin complexed with its carbohydrate phosphate inhibitors suggests its substrate/receptor recognition., Chou CC, Sun YJ, Meng M, Hsiao CD, J Biol Chem. 2000 Jul 28;275(30):23154-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10770936 10770936]
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[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
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[[Category: Glucose-6-phosphate isomerase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Chen W-S]]
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[[Category: Chen, W S.]]
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[[Category: Chou C-C]]
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[[Category: Chou, C C.]]
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[[Category: Hsiao C-D]]
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[[Category: Hsiao, C D.]]
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[[Category: Meng M]]
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[[Category: Meng, M.]]
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[[Category: Sun Y-J]]
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[[Category: Sun, Y J.]]
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[[Category: autocrinefactor]]
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[[Category: crystallography motility]]
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[[Category: neuroleukin]]
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[[Category: phosphoglucose isomerase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:51:30 2008''
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Current revision

The crystal structure of phosphoglucose isomerase-an enzyme with autocrine motility factor activity in tumor cells

PDB ID 1b0z

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