View source for 2wfa


==Structure of Beta-Phosphoglucomutase inhibited with Beryllium trifluoride, in an open conformation.==
<StructureSection load='2wfa' size='340' side='right'caption='[[2wfa]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2wfa]] 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=2WFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WFA 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]] 1.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</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=2wfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wfa OCA], [https://pdbe.org/2wfa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wfa RCSB], [https://www.ebi.ac.uk/pdbsum/2wfa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wfa 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/wf/2wfa_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=2wfa ConSurf].
<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
Experimental observations of fluoromagnesate and fluoroaluminate complexes of beta-phosphoglucomutase (beta-PGM) have demonstrated the importance of charge balance in transition-state stabilization for phosphoryl transfer enzymes. Here, direct observations of ground-state analog complexes of beta-PGM involving trifluoroberyllate establish that when the geometry and charge distribution closely match those of the substrate, the distribution of conformers in solution and in the crystal predominantly places the reacting centers in van der Waals proximity. Importantly, two variants are found, both of which satisfy the criteria for near attack conformers. In one variant, the aspartate general base for the reaction is remote from the nucleophile. The nucleophile remains protonated and forms a nonproductive hydrogen bond to the phosphate surrogate. In the other variant, the general base forms a hydrogen bond to the nucleophile that is now correctly orientated for the chemical transfer step. By contrast, in the absence of substrate, the solvent surrounding the phosphate surrogate is arranged to disfavor nucleophilic attack by water. Taken together, the trifluoroberyllate complexes of beta-PGM provide a picture of how the enzyme is able to organize itself for the chemical step in catalysis through the population of intermediates that respond to increasing proximity of the nucleophile. These experimental observations show how the enzyme is capable of stabilizing the reaction pathway toward the transition state and also of minimizing unproductive catalysis of aspartyl phosphate hydrolysis.

Near attack conformers dominate beta-phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate.,Griffin JL, Bowler MW, Baxter NJ, Leigh KN, Dannatt HR, Hounslow AM, Blackburn GM, Webster CE, Cliff MJ, Waltho JP Proc Natl Acad Sci U S A. 2012 May 1;109(18):6910-5. Epub 2012 Apr 13. PMID:22505741<ref>PMID:22505741</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2wfa" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-phosphoglucomutase 3D structures|Beta-phosphoglucomutase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lactococcus lactis]]
[[Category: Large Structures]]
[[Category: Alizadeh T]]
[[Category: Baxter NJ]]
[[Category: Bermel W]]
[[Category: Blackburn GM]]
[[Category: Bowler MW]]
[[Category: Cliff MJ]]
[[Category: Hollfelder F]]
[[Category: Hounslow AM]]
[[Category: Pollard S]]
[[Category: Waltho JP]]
[[Category: Webster CE]]
[[Category: Williams NH]]