1o08
From Proteopedia
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(New page: 200px<br /><applet load="1o08" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o08, resolution 1.20Å" /> '''Structure of Pentava...) |
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| - | [[Image:1o08.gif|left|200px]]<br /><applet load="1o08" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1o08, resolution 1.20Å" /> | ||
| - | '''Structure of Pentavalent Phosphorous Intermediate of an Enzyme Catalyzed Phosphoryl transfer Reaction observed on cocrystallization with Glucose 1-phosphate'''<br /> | ||
| - | == | + | ==Structure of Pentavalent Phosphorous Intermediate of an Enzyme Catalyzed Phosphoryl transfer Reaction observed on cocrystallization with Glucose 1-phosphate== |
| - | Enzymes provide enormous rate enhancements, unmatched by any other type of | + | <StructureSection load='1o08' size='340' side='right'caption='[[1o08]], [[Resolution|resolution]] 1.20Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1o08]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O08 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O08 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]] 1.2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G16:ALPHA-D-GLUCOSE+1,6-BISPHOSPHATE'>G16</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1o08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o08 OCA], [https://pdbe.org/1o08 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o08 RCSB], [https://www.ebi.ac.uk/pdbsum/1o08 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o08 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PGMB_LACLA PGMB_LACLA] Catalyzes the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate. The beta-phosphoglucomutase (Beta-PGM) acts on the beta-C(1) anomer of G1P. Glucose or lactose are used in preference to maltose, which is only utilized after glucose or lactose has been exhausted. It plays a key role in the regulation of the flow of carbohydrate intermediates in glycolysis and the formation of the sugar nucleotide UDP-glucose.<ref>PMID:9084169</ref> <ref>PMID:15005616</ref> | ||
| + | == 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/o0/1o08_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1o08 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Enzymes provide enormous rate enhancements, unmatched by any other type of catalyst. The stabilization of high-energy states along the reaction coordinate is the crux of the catalytic power of enzymes. We report the atomic-resolution structure of a high-energy reaction intermediate stabilized in the active site of an enzyme. Crystallization of phosphorylated beta-phosphoglucomutase in the presence of the Mg(II) cofactor and either of the substrates glucose 1-phosphate or glucose 6-phosphate produced crystals of the enzyme-Mg(II)-glucose 1,6-(bis)phosphate complex, which diffracted x-rays to 1.2 and 1.4 angstroms, respectively. The structure reveals a stabilized pentacovalent phosphorane formed in the phosphoryl transfer from the C(1)O of glucose 1,6-(bis)phosphate to the nucleophilic Asp8 carboxylate. | ||
| - | + | The pentacovalent phosphorus intermediate of a phosphoryl transfer reaction.,Lahiri SD, Zhang G, Dunaway-Mariano D, Allen KN Science. 2003 Mar 28;299(5615):2067-71. Epub 2003 Mar 13. PMID:12637673<ref>PMID:12637673</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1o08" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Beta-phosphoglucomutase 3D structures|Beta-phosphoglucomutase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Lactococcus lactis]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Allen KN]] | ||
| + | [[Category: Dunaway-Mariano D]] | ||
| + | [[Category: Lahiri SD]] | ||
| + | [[Category: Zhang G]] | ||
Current revision
Structure of Pentavalent Phosphorous Intermediate of an Enzyme Catalyzed Phosphoryl transfer Reaction observed on cocrystallization with Glucose 1-phosphate
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