1o08: Difference between revisions

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New page: left|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 1.20&Aring;" />
'''Structure of Pentavalent Phosphorous Intermediate of an Enzyme Catalyzed Phosphoryl transfer Reaction observed on cocrystallization with Glucose 1-phosphate'''<br />


==Overview==
==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, 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.
<StructureSection load='1o08' size='340' side='right'caption='[[1o08]], [[Resolution|resolution]] 1.20&Aring;' 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]] 1.2&#8491;</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.


==About this Structure==
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>
1O08 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis] with G16 and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Beta-phosphoglucomutase Beta-phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.6 5.4.2.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O08 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12637673 12637673]
</div>
[[Category: Beta-phosphoglucomutase]]
<div class="pdbe-citations 1o08" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Beta-phosphoglucomutase 3D structures|Beta-phosphoglucomutase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lactococcus lactis]]
[[Category: Lactococcus lactis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Allen, K.N.]]
[[Category: Allen KN]]
[[Category: Dunaway-Mariano, D.]]
[[Category: Dunaway-Mariano D]]
[[Category: Lahiri, S.D.]]
[[Category: Lahiri SD]]
[[Category: Zhang, G.]]
[[Category: Zhang G]]
[[Category: G16]]
[[Category: MG]]
[[Category: haloacid dehalogenase superfamily]]
[[Category: pentavalent phosphate intermediate]]
[[Category: phosphotransferase]]
 
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