1gyy

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[[Image:1gyy.gif|left|200px]]<br /><applet load="1gyy" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gyy, resolution 1.35&Aring;" />
 
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'''THE CRYSTAL STRUCTURE OF YDCE, A 4-OXALOCROTONATE TAUTOMERASE HOMOLOGUE FROM ESCHERICHIA COLI, CONFIRMS THE STRUCTURAL BASIS FOR OLIGOMER DIVERSITY'''<br />
 
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==Overview==
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==The Crystal Structure of YdcE, a 4-Oxalocrotonate Tautomerase Homologue from Escherichia coli, Confirms the Structural Basis for Oligomer Diversity==
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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.
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<StructureSection load='1gyy' size='340' side='right'caption='[[1gyy]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1gyy]] is a 2 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=1GYY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GYY FirstGlance]. <br>
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1GYY 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 <scene name='pdbligand=FHC:'>FHC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Known structural/functional Site: <scene name='pdbsite=FHA:Fhc+Binding+Site+For+Chain+B'>FHA</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GYY OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FHC:2-FLUORO-3-(4-HYDROXYPHENYL)-2E-PROPENEOATE'>FHC</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gyy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gyy OCA], [https://pdbe.org/1gyy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gyy RCSB], [https://www.ebi.ac.uk/pdbsum/1gyy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gyy ProSAT]</span></td></tr>
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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]
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gy/1gyy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1gyy ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Phenylpyruvate tautomerase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Almrud J]]
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[[Category: Almrud, J.]]
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[[Category: Czerwinski R]]
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[[Category: Czerwinski, R.]]
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[[Category: Hackert M]]
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[[Category: Hackert, M.]]
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[[Category: Johnson W]]
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[[Category: Johnson, W.]]
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[[Category: Kern A]]
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[[Category: Kern, A.]]
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[[Category: Murzin A]]
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[[Category: Murzin, A.]]
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[[Category: Wang S]]
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[[Category: Wang, S.]]
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[[Category: Whitman C]]
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[[Category: Whitman, C.]]
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[[Category: FHC]]
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[[Category: complete prote]]
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[[Category: hypothetical protein]]
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[[Category: isomerase]]
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[[Category: tautomerase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:55:30 2008''
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Current revision

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

PDB ID 1gyy

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