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New page: left|200px<br /><applet load="1gyj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gyj, resolution 2.1Å" /> '''THE CRYSTAL STRUCTURE...
 
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[[Image:1gyj.jpg|left|200px]]<br /><applet load="1gyj" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1gyj, resolution 2.1&Aring;" />
'''THE CRYSTAL STRUCTURE OF YDCE, A 4-OXALOCROTONATE TAUTOMERASE HOMOLOGUE FROM ESCHERICHIA COLI, CONFIRMS THE STRUCTURAL BASIS FOR OLIGOMER DIVERSITY'''<br />


==Overview==
==The Crystal Structure of YdcE, a 4-Oxalocrotonate Tautomerase Homologue from Escherichia coli, Confirms the Structural Basis for Oligomer Diversity==
The tautomerase superfamily consists of three major families represented, by 4-oxalocrotonate tautomerase (4-OT), 5-(carboxymethyl)-2-hydroxymuconate isomerase (CHMI), and macrophage, migration inhibitory factor (MIF). The members of this superfamily are, structurally homologous proteins constructed from a simple beta-alpha-beta, fold that share a key mechanistic feature; they use an amino-terminal, proline, which has an unusually low pK(a), as the general base in a, keto-enol tautomerization. Several new members of the 4-OT family have now, been identified using PSI-BLAST and categorized into five subfamilies on, the basis of multiple-sequence alignments and the conservation of key, catalytic and structural residues. The members of subfamily 5, which, includes a hypothetical protein designated YdcE from Escherichia coli, are, predicted not to form hexamers. The crystal structure of YdcE has been, determined to 1.35 A resolution and confirms that it is a dimer. In, addition, YdcE complexed with (E)-2-fluoro-p-hydroxycinnamate, identified, as a potent competitive inhibitor of this enzyme, as well as, N-(2-hydroxyethyl)piperazine-N'-2-ethanesulfonic acid (HEPES) and benzoate, are also presented. These latter crystal structures reveal the location of, the active site and suggest a mechanism for the observed YdcE-catalyzed, tautomerization reaction. The dimeric arrangement of YdcE represents a new, structure in the 4-OT family and demonstrates structural diversity within, the 4-OT family not previously reported.
<StructureSection load='1gyj' size='340' side='right'caption='[[1gyj]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1gyj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GYJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GYJ FirstGlance]. <br>
1GYJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Phenylpyruvate_tautomerase Phenylpyruvate tautomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.2.1 5.3.2.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GYJ 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]] 2.1&#8491;</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=1gyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gyj OCA], [https://pdbe.org/1gyj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gyj RCSB], [https://www.ebi.ac.uk/pdbsum/1gyj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gyj ProSAT]</span></td></tr>
==Reference==
</table>
The crystal structure of YdcE, a 4-oxalocrotonate tautomerase homologue from Escherichia coli, confirms the structural basis for oligomer diversity., Almrud JJ, Kern AD, Wang SC, Czerwinski RM, Johnson WH Jr, Murzin AG, Hackert ML, Whitman CP, Biochemistry. 2002 Oct 8;41(40):12010-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12356301 12356301]
== Function ==
[[Category: Escherichia coli]]
[https://www.uniprot.org/uniprot/PPTA_ECOLI PPTA_ECOLI] Can use enol isomers of phenylpyruvate, 2-hydroxy-2,4-pentadienoate and (p-hydroxyphenyl)pyruvate as substrates.<ref>PMID:12356301</ref>
[[Category: Phenylpyruvate tautomerase]]
== Evolutionary Conservation ==
[[Category: Single protein]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Almrud, J.]]
Check<jmol>
[[Category: Czerwinski, R.]]
  <jmolCheckbox>
[[Category: Hackert, M.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gy/1gyj_consurf.spt"</scriptWhenChecked>
[[Category: Johnson, W.]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: Kern, A.]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: Murzin, A.]]
  </jmolCheckbox>
[[Category: Wang, S.]]
</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=1gyj ConSurf].
[[Category: Whitman, C.]]
<div style="clear:both"></div>
[[Category: complete proteome]]
== References ==
[[Category: hypothetical protein]]
<references/>
[[Category: isomerase]]
__TOC__
[[Category: tautomerase]]
</StructureSection>
 
[[Category: Escherichia coli K-12]]
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:20:53 2007''
[[Category: Large Structures]]
[[Category: Almrud J]]
[[Category: Czerwinski R]]
[[Category: Hackert M]]
[[Category: Johnson W]]
[[Category: Kern A]]
[[Category: Murzin A]]
[[Category: Wang S]]
[[Category: Whitman C]]

Latest revision as of 11:25, 27 March 2024

The Crystal Structure of YdcE, a 4-Oxalocrotonate Tautomerase Homologue from Escherichia coli, Confirms the Structural Basis for Oligomer Diversity

1gyj, resolution 2.10Å

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