1yns

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[[Image:1yns.gif|left|200px]]<br /><applet load="1yns" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1yns, resolution 1.7&Aring;" />
 
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'''Crystal Structure Of Human Enolase-phosphatase E1 and its complex with a substrate analog'''<br />
 
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==Overview==
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==Crystal Structure Of Human Enolase-phosphatase E1 and its complex with a substrate analog==
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Enolase-phosphatase E1 (MASA) is a bifunctional enzyme in the ubiquitous methionine salvage pathway that catalyzes the continuous reactions of 2,3-diketo-5-methylthio-1-phosphopentane to yield the aci-reductone metabolite using Mg2+ as cofactor. In this study, we have determined the crystal structure of MASA and its complex with a substrate analog to 1.7A resolution by multi-wavelength anomalous diffraction and molecular replacement techniques, respectively. The structures support the proposed mechanism of phosphatase activity and further suggest the probable mechanism of enolization. We establish a model for substrate binding to describe in detail the enzymatic reaction and the formation of the transition state, which will provide insight into the reaction mechanisms of other enzymes in the same family.
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<StructureSection load='1yns' size='340' side='right'caption='[[1yns]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1yns]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YNS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YNS FirstGlance]. <br>
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1YNS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=HPO:'>HPO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YNS 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]] 1.7&#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=HPO:2-OXOHEPTYLPHOSPHONIC+ACID'>HPO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1yns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yns OCA], [https://pdbe.org/1yns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yns RCSB], [https://www.ebi.ac.uk/pdbsum/1yns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yns ProSAT]</span></td></tr>
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Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity., Wang H, Pang H, Bartlam M, Rao Z, J Mol Biol. 2005 May 13;348(4):917-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15843022 15843022]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ENOPH_HUMAN ENOPH_HUMAN] Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).<ref>PMID:15843022</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/yn/1yns_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=1yns 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: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bartlam, M.]]
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[[Category: Bartlam M]]
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[[Category: Pang, H.]]
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[[Category: Pang H]]
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[[Category: Rao, Z.]]
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[[Category: Rao Z]]
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[[Category: Wang, H.]]
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[[Category: Wang H]]
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[[Category: HPO]]
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[[Category: MG]]
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[[Category: hydrolase fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:07:14 2008''
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Current revision

Crystal Structure Of Human Enolase-phosphatase E1 and its complex with a substrate analog

PDB ID 1yns

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