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| [[Image:1dub.jpg|left|200px]]
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| {{Structure
| | ==2-ENOYL-COA HYDRATASE, DATA COLLECTED AT 100 K, PH 6.5== |
| |PDB= 1dub |SIZE=350|CAPTION= <scene name='initialview01'>1dub</scene>, resolution 2.5Å
| | <StructureSection load='1dub' size='340' side='right'caption='[[1dub]], [[Resolution|resolution]] 2.50Å' scene=''> |
| |SITE= <scene name='pdbsite=CR1:Catalytic+Residue+1'>CR1</scene> and <scene name='pdbsite=CR2:Catalytic+Residue+2'>CR2</scene>
| | == Structural highlights == |
| |LIGAND= <scene name='pdbligand=CAA:ACETOACETYL-COENZYME+A'>CAA</scene>
| | <table><tr><td colspan='2'>[[1dub]] 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=1DUB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DUB FirstGlance]. <br> |
| |ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| |GENE= | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAA:ACETOACETYL-COENZYME+A'>CAA</scene></td></tr> |
| |DOMAIN=
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dub OCA], [https://pdbe.org/1dub PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dub RCSB], [https://www.ebi.ac.uk/pdbsum/1dub PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dub ProSAT]</span></td></tr> |
| |RELATEDENTRY=
| | </table> |
| |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dub OCA], [http://www.ebi.ac.uk/pdbsum/1dub PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dub RCSB]</span>
| | == Function == |
| }}
| | [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]] |
| | Check<jmol> |
| | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/du/1dub_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> |
| | </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=1dub ConSurf]. |
| | <div style="clear:both"></div> |
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| '''2-ENOYL-COA HYDRATASE, DATA COLLECTED AT 100 K, PH 6.5'''
| | ==See Also== |
| | | *[[Enoyl-CoA hydratase 3D structures|Enoyl-CoA hydratase 3D structures]] |
| | | __TOC__ |
| ==Overview== | | </StructureSection> |
| The crystal structure of rat liver mitochondrial enoyl-coenzyme A (CoA) hydratase complexed with the potent inhibitor acetoacetyl-CoA has been refined at 2.5 angstroms resolution. This enzyme catalyses the reversible addition of water to alpha,beta-unsaturated enoyl-CoA thioesters, with nearly diffusion-controlled reaction rates for the best substrates. Enoyl-CoA hydratase is a hexamer of six identical subunits of 161 kDa molecular mass for the complex. The hexamer is a dimer of trimers. The monomer is folded into a right-handed spiral of four turns, followed by two small domains which are involved in trimerization. Each turn of the spiral consists of two beta-strands and an alpha-helix. The mechanism for the hydratase/dehydratase reaction follows a syn-stereochemistry, a preference that is opposite to the nonenzymatic reaction. The active-site architecture agrees with this stereochemistry. It confirms the importance of Glu164 as the catalytic acid for providing the alpha-proton during the hydratase reaction. It also shows the importance of Glu144 as the catalytic base for the activation of a water molecule in the hydratase reaction. The comparison of an unliganded and a liganded active site within the same crystal form shows a water molecule in the unliganded subunit. This water molecule is bound between the two catalytic glutamates and could serve as the activated water during catalysis.
| | [[Category: Large Structures]] |
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| ==About this Structure==
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| 1DUB is a [[Single protein]] structure of 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=1DUB OCA].
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| ==Reference==
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| Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: a spiral fold defines the CoA-binding pocket., Engel CK, Mathieu M, Zeelen JP, Hiltunen JK, Wierenga RK, EMBO J. 1996 Oct 1;15(19):5135-45. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8895557 8895557]
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| [[Category: Enoyl-CoA hydratase]] | |
| [[Category: Rattus norvegicus]] | | [[Category: Rattus norvegicus]] |
| [[Category: Single protein]]
| | [[Category: Engel CK]] |
| [[Category: Engel, C K.]] | | [[Category: Wierenga RK]] |
| [[Category: Wierenga, R K.]] | |
| [[Category: beta-oxidation]]
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| [[Category: coa]]
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| [[Category: crotonase]]
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| [[Category: enoyl-coa hydratase]]
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| [[Category: fatty acid metabolism]]
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| [[Category: lyase]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:48:47 2008''
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