1mj3: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1mj3]] is a 6 chain structure with sequence from [http://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 [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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MJ3 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HXC:HEXANOYL-COENZYME+A'>HXC</scene>< | </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> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dub|1dub]], [[2dub|2dub]], [[1ey3|1ey3]]</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><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='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><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://www.rcsb.org/pdb/explore.do?structureId=1mj3 RCSB], [http://www.ebi.ac.uk/pdbsum/1mj3 PDBsum]</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://www.rcsb.org/pdb/explore.do?structureId=1mj3 RCSB], [http://www.ebi.ac.uk/pdbsum/1mj3 PDBsum]</span></td></tr> | ||
<table> | </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. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Enoyl-CoA hydratase]] | [[Category: Enoyl-CoA hydratase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Bell, A F | [[Category: Bell, A F]] | ||
[[Category: Feng, Y | [[Category: Feng, Y]] | ||
[[Category: Hofstein, H A | [[Category: Hofstein, H A]] | ||
[[Category: Kisker, C | [[Category: Kisker, C]] | ||
[[Category: Parikh, S | [[Category: Parikh, S]] | ||
[[Category: Rudolph, M J | [[Category: Rudolph, M J]] | ||
[[Category: Tonge, P J | [[Category: Tonge, P J]] | ||
[[Category: Wu, J | [[Category: Wu, J]] | ||
[[Category: Homohexamer]] | [[Category: Homohexamer]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
Revision as of 13:29, 25 December 2014
Crystal Structure Analysis of rat enoyl-CoA hydratase in complex with hexadienoyl-CoACrystal Structure Analysis of rat enoyl-CoA hydratase in complex with hexadienoyl-CoA
Structural highlights
Function[ECHM_RAT] Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedEnoyl-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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