1egh: Difference between revisions

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New page: left|200px<br /><applet load="1egh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1egh, resolution 2.00Å" /> '''STRUCTURE OF METHYLG...
 
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[[Image:1egh.gif|left|200px]]<br /><applet load="1egh" size="450" color="white" frame="true" align="right" spinBox="true"
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'''STRUCTURE OF METHYLGLYOXAL SYNTHASE COMPLEXED WITH THE COMPETITIVE INHIBITOR 2-PHOSPHOGLYCOLATE'''<br />


==Overview==
==STRUCTURE OF METHYLGLYOXAL SYNTHASE COMPLEXED WITH THE COMPETITIVE INHIBITOR 2-PHOSPHOGLYCOLATE==
The crystal structure of the transition-state analogue 2-phosphoglycolate, (2PG) bound to methylglyoxal synthase (MGS) is presented at a resolution, of 2.0 A. This structure is very similar to the previously determined, structure of MGS complexed to formate and phosphate. Since 2PG is a, competitive inhibitor of both MGS and triosephosphate isomerase (TIM), the, carboxylate groups of each bound 2PG from this structure and the structure, of 2PG bound to TIM were used to align and compare the active sites, despite differences in their protein folds. The distances between the, functional groups of Asp 71, His 98, His 19, and the carboxylate oxygens, of the 2PG molecule in MGS are similar to the corresponding distances, between the functional groups of Glu 165, His 95, Lys 13, and the, carboxylate oxygens of the 2PG molecule in TIM. However, these spatial, relationships are enantiomorphic to each other. Consistent with the known, stereochemical data, the catalytic base Asp 71 is positioned on the, opposite face of the 2PG-carboxylate plane as Glu 165 of TIM. Both His 98, of MGS and His 95 of TIM are in the plane of the carboxylate of 2PG, suggesting that these two residues are homologous in function. While His, 19 of MGS and Lys 13 of TIM appear on the opposite face of the 2PG, carboxylate plane, their relative location to the 2PG molecule is quite, different, suggesting that they probably have different functions. Most, remarkably, unlike the coplanar structure found in the 2PG molecule bound, to TIM, the torsion angle around the C1-C2 bond of 2PG bound to MGS brings, the phosphoryl moiety out of the molecule's carboxylate plane, facilitating elimination. Further, the superimposition of this structure, with the structure of MGS bound to formate and phosphate suggests a model, for the enzyme bound to the first transition state.
<StructureSection load='1egh' size='340' side='right'caption='[[1egh]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1egh]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EGH FirstGlance]. <br>
1EGH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PGA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Methylglyoxal_synthase Methylglyoxal synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.3 4.2.3.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EGH OCA].  
</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&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1egh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egh OCA], [https://pdbe.org/1egh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1egh RCSB], [https://www.ebi.ac.uk/pdbsum/1egh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1egh ProSAT]</span></td></tr>
Mirroring perfection: the structure of methylglyoxal synthase complexed with the competitive inhibitor 2-phosphoglycolate., Saadat D, Harrison DH, Biochemistry. 2000 Mar 21;39(11):2950-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10715115 10715115]
</table>
== Function ==
[https://www.uniprot.org/uniprot/MGSA_ECOLI MGSA_ECOLI]
== 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/eg/1egh_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/main_output.php?pdb_ID=1egh ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Methylglyoxal synthase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Harrison DHT]]
[[Category: Harrison, D.H.T.]]
[[Category: Saadat D]]
[[Category: Saadat, D.]]
[[Category: PGA]]
[[Category: beta/alpha protein]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:59:14 2007''

Latest revision as of 10:02, 7 February 2024

STRUCTURE OF METHYLGLYOXAL SYNTHASE COMPLEXED WITH THE COMPETITIVE INHIBITOR 2-PHOSPHOGLYCOLATESTRUCTURE OF METHYLGLYOXAL SYNTHASE COMPLEXED WITH THE COMPETITIVE INHIBITOR 2-PHOSPHOGLYCOLATE

Structural highlights

1egh is a 6 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MGSA_ECOLI

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1egh, resolution 2.00Å

Drag the structure with the mouse to rotate

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OCA
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