1mj3: Difference between revisions

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 ==Crystal Structure Analysis of rat enoyl-CoA hydratase in complex with hexadienoyl-CoA==
-<StructureSection load='1mj3' size='340' side='right' caption='[[1mj3]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+<StructureSection load='1mj3' size='340' side='right'caption='[[1mj3]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mj3]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MJ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MJ3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mj3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MJ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MJ3 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HXC:HEXANOYL-COENZYME+A'>HXC</scene></td></tr>
+</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dub|1dub]], [[2dub|2dub]], [[1ey3|1ey3]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HXC:HEXANOYL-COENZYME+A'>HXC</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Enoyl-CoA_hydratase Enoyl-CoA hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.17 4.2.1.17] </span></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=1mj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mj3 OCA], [https://pdbe.org/1mj3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mj3 RCSB], [https://www.ebi.ac.uk/pdbsum/1mj3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mj3 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mj3 OCA], [http://pdbe.org/1mj3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mj3 RCSB], [http://www.ebi.ac.uk/pdbsum/1mj3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mj3 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ECHM_RAT ECHM_RAT]] Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate.
+[https://www.uniprot.org/uniprot/ECHM_RAT ECHM_RAT] Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 21: / Line 20: @@
 </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=1mj3 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Enoyl-CoA hydratase catalyzes the hydration of trans-2-crotonyl-CoA to 3(S)- and 3(R)-hydroxybutyryl-CoA with a stereoselectivity (3(S)/3(R)) of 400,000 to 1. Importantly, Raman spectroscopy reveals that both the s-cis and s-trans conformers of the substrate analog hexadienoyl-CoA are bound to the enzyme, but that only the s-cis conformer is polarized. This selective polarization is an example of ground state strain, indicating the existence of catalytically relevant ground state destabilization arising from the selective complementarity of the enzyme toward the transition state rather than the ground state. Consequently, the stereoselectivity of the enzyme-catalyzed reaction results from the selective activation of one of two bound substrate conformers rather than from selective binding of a single conformer. These findings have important implications for inhibitor design and the role of ground state interactions in enzyme catalysis.
-Stereoselectivity of enoyl-CoA hydratase results from preferential activation of one of two bound substrate conformers.,Bell AF, Feng Y, Hofstein HA, Parikh S, Wu J, Rudolph MJ, Kisker C, Whitty A, Tonge PJ Chem Biol. 2002 Nov;9(11):1247-55. PMID:12445775<ref>PMID:12445775</ref>
+==See Also==
+*[[Enoyl-CoA hydratase|Enoyl-CoA hydratase]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+*[[Enoyl-CoA hydratase 3D structures|Enoyl-CoA hydratase 3D structures]]
-</div>
-<div class="pdbe-citations 1mj3" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
+[[Category: Large Structures]]
-[[Category: Enoyl-CoA hydratase]]
+[[Category: Rattus norvegicus]]
-[[Category: Bell, A F]]
+[[Category: Bell AF]]
-[[Category: Feng, Y]]
+[[Category: Feng Y]]
-[[Category: Hofstein, H A]]
+[[Category: Hofstein HA]]
-[[Category: Kisker, C]]
+[[Category: Kisker C]]
-[[Category: Parikh, S]]
+[[Category: Parikh S]]
-[[Category: Rudolph, M J]]
+[[Category: Rudolph MJ]]
-[[Category: Tonge, P J]]
+[[Category: Tonge PJ]]
-[[Category: Wu, J]]
+[[Category: Wu J]]
-[[Category: Homohexamer]]
-[[Category: Lyase]]