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New page: left|200px<br /><applet load="1eun" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eun, resolution 2.00Å" /> '''STRUCTURE OF 2-KETO-...
 
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[[Image:1eun.gif|left|200px]]<br /><applet load="1eun" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1eun, resolution 2.00&Aring;" />
'''STRUCTURE OF 2-KETO-3-DEOXY-6-PHOSPHOGLUCONATE ALDOLASE FROM ESCHERICHIA COLI'''<br />


==Overview==
==STRUCTURE OF 2-KETO-3-DEOXY-6-PHOSPHOGLUCONATE ALDOLASE FROM ESCHERICHIA COLI==
2-Keto-3-deoxy-6-phosphogluconate (KDPG) aldolase catalyzes the reversible, cleavage of KDPG to pyruvate and glyceraldehyde-3-phosphate. The enzyme is, a class I aldolase whose reaction mechanism involves formation of Schiff, base intermediates between Lys-133 and a keto substrate. A covalent adduct, was trapped by flash freezing KDPG aldolase crystals soaked with 10 mM, pyruvate in acidic conditions at pH 4.6. Structure determination to 1.95-A, resolution showed that pyruvate had undergone nucleophilic attack with, Lys-133, forming a protonated carbinolamine intermediate, a functional, Schiff base precursor, which was stabilized by hydrogen bonding with, active site residues. Carbinolamine interaction with Glu-45 indicates, general base catalysis of several rate steps. Stereospecific addition is, ensured by aromatic interaction of Phe-135 with the pyruvate methyl group., In the native structure, Lys-133 donates all of its hydrogen bonds, indicating the presence of an epsilon-ammonium salt group. Nucleophilic, activation is postulated to occur by proton transfer in the monoprotonated, zwitterionic pair (Glu-45/Lys-133). Formation of the zwitterionic pair, requires prior side chain rearrangement by protonated Lys-133 to displace, a water molecule, hydrogen bonded to the zwitterionic residues.
<StructureSection load='1eun' size='340' side='right'caption='[[1eun]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1eun]] is a 3 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=1EUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EUN 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]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1eun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eun OCA], [https://pdbe.org/1eun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eun RCSB], [https://www.ebi.ac.uk/pdbsum/1eun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eun ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ALKH_ECOLI ALKH_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/eu/1eun_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=1eun ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1EUN 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 SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/2-dehydro-3-deoxy-phosphogluconate_aldolase 2-dehydro-3-deoxy-phosphogluconate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.14 4.1.2.14] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EUN OCA].
*[[Aldolase 3D structures|Aldolase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Covalent intermediate trapped in 2-keto-3-deoxy-6- phosphogluconate (KDPG) aldolase structure at 1.95-A resolution., Allard J, Grochulski P, Sygusch J, Proc Natl Acad Sci U S A. 2001 Mar 27;98(7):3679-84. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11274385 11274385]
[[Category: 2-dehydro-3-deoxy-phosphogluconate aldolase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Allard, J.]]
[[Category: Allard J]]
[[Category: Grochulski, P.]]
[[Category: Grochulski P]]
[[Category: Sygusch, J.]]
[[Category: Sygusch J]]
[[Category: SO4]]
[[Category: 2-keto-3-deoxy-6-phosphogluconate aldolase]]
[[Category: beta-barrel]]
[[Category: sulfate]]
[[Category: trimer]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:19:52 2007''

Latest revision as of 07:07, 7 February 2024

STRUCTURE OF 2-KETO-3-DEOXY-6-PHOSPHOGLUCONATE ALDOLASE FROM ESCHERICHIA COLI

1eun, resolution 2.00Å

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