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1pn2

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(New page: 200px<br /><applet load="1pn2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pn2, resolution 1.95&Aring;" /> '''Crystal structure an...)
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[[Image:1pn2.jpg|left|200px]]<br /><applet load="1pn2" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1pn2, resolution 1.95&Aring;" />
 
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'''Crystal structure analysis of the selenomethionine labelled 2-enoyl-CoA hydratase 2 domain of Candida tropicalis multifunctional enzyme type 2'''<br />
 
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==Overview==
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==Crystal structure analysis of the selenomethionine labelled 2-enoyl-CoA hydratase 2 domain of Candida tropicalis multifunctional enzyme type 2==
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2-Enoyl-CoA hydratase 2, a part from multifunctional enzyme type 2, hydrates trans-2-enoyl-CoA to 3-hydroxyacyl-CoA in the, (3R)-hydroxy-dependent route of peroxisomal beta-oxidation of fatty acids., Unliganded and (3R)-hydroxydecanoyl coenzyme A-complexed crystal, structures of 2-enoyl-CoA hydratase 2 from Candida tropicalis, multifunctional enzyme type 2 were solved to 1.95- and 2.35-A resolution, respectively. 2-Enoyl-CoA hydratase 2 is a dimeric, alpha+beta protein, with a novel quaternary structure. The overall structure of the two-domain, subunit of eukaryotic 2-enoyl-CoA hydratase 2 resembles the homodimeric, hot dog fold structures of prokaryotic (R)-specific 2-enoyl-CoA hydratase, and beta-hydroxydecanoyl thiol ester dehydrase. Importantly, though, the, eukaryotic hydratase 2 has a complete hot dog fold only in its C-domain, whereas the N-domain lacks a long central alpha-helix, thus creating space, for bulkier substrates in the binding pocket and explaining the observed, difference in substrate preference between eukaryotic and prokaryotic, enzymes. Although the N- and C-domains have an identity of &lt;10% at the, amino acid level, they share a 50% identity at the nucleotide level and, fold similarly. We suggest that a subunit of 2-enoyl-CoA hydratase 2 has, evolved via a gene duplication with the concomitant loss of one catalytic, site. The hydrogen bonding network of the active site of 2-enoyl-CoA, hydratase 2 resembles the active site geometry of mitochondrial, (S)-specific 2-enoyl-CoA hydratase 1, although in a mirror image fashion., This arrangement allows the reaction to occur by similar mechanism, supported by mutagenesis and mechanistic studies, although via reciprocal, stereochemistry.
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<StructureSection load='1pn2' size='340' side='right'caption='[[1pn2]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1pn2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_tropicalis Candida tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PN2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PN2 FirstGlance]. <br>
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1PN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_tropicalis Candida tropicalis] with EDO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PN2 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]] 1.95&#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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1pn2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pn2 OCA], [https://pdbe.org/1pn2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pn2 RCSB], [https://www.ebi.ac.uk/pdbsum/1pn2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pn2 ProSAT]</span></td></tr>
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A two-domain structure of one subunit explains unique features of eukaryotic hydratase 2., Koski MK, Haapalainen AM, Hiltunen JK, Glumoff T, J Biol Chem. 2004 Jun 4;279(23):24666-72. Epub 2004 Mar 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15051722 15051722]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FOX2_CANTR FOX2_CANTR] Second trifunctional enzyme acting on the beta-oxidation pathway for fatty acids, possessing hydratase-dehydrogenase-epimerase activities. Converts trans-2-enoyl-CoA via D-3-hydroxyacyl-CoA to 3-ketoacyl-CoA.
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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/pn/1pn2_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=1pn2 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Candida tropicalis]]
[[Category: Candida tropicalis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Glumoff, T.]]
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[[Category: Glumoff T]]
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[[Category: Haapalainen, A.M.]]
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[[Category: Haapalainen AM]]
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[[Category: Hiltunen, J.K.]]
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[[Category: Hiltunen JK]]
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[[Category: Koski, M.K.]]
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[[Category: Koski MK]]
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[[Category: EDO]]
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[[Category: hot-dog fold]]
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[[Category: hydratase 2 motif]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:56:04 2007''
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Current revision

Crystal structure analysis of the selenomethionine labelled 2-enoyl-CoA hydratase 2 domain of Candida tropicalis multifunctional enzyme type 2

PDB ID 1pn2

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