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2wfa: Difference between revisions

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[[Image:2wfa.png|left|200px]]
==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 [http://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]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1z4o|1z4o]], [[2wf5|2wf5]], [[1o03|1o03]], [[1zol|1zol]], [[1z4n|1z4n]], [[1lvh|1lvh]], [[1o08|1o08]], [[2wf6|2wf6]], [[2wf8|2wf8]], [[2wf7|2wf7]], [[2wf9|2wf9]]</td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wfa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wfa RCSB], [http://www.ebi.ac.uk/pdbsum/2wfa PDBsum]</span></td></tr>
<table>
== 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/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


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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>
The line below this paragraph, containing "STRUCTURE_2wfa", creates the "Structure Box" on the page.
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{{STRUCTURE_2wfa|  PDB=2wfa  |  SCENE=  }}


===Structure of Beta-Phosphoglucomutase inhibited with Beryllium trifluoride, in an open conformation.===
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
 
</div>
 
== References ==
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<references/>
The line below this paragraph, {{ABSTRACT_PUBMED_22505741}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 22505741 is the PubMed ID number.
</StructureSection>
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{{ABSTRACT_PUBMED_22505741}}
 
==About this Structure==
[[2wfa]] is a 1 chain structure with sequence from [http://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].
 
==Reference==
<ref group="xtra">PMID:022505741</ref><references group="xtra"/>
[[Category: Beta-phosphoglucomutase]]
[[Category: Beta-phosphoglucomutase]]
[[Category: Lactococcus lactis]]
[[Category: Lactococcus lactis]]

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