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| | <StructureSection load='1pn4' size='340' side='right'caption='[[1pn4]], [[Resolution|resolution]] 2.35Å' scene=''> | | <StructureSection load='1pn4' size='340' side='right'caption='[[1pn4]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1pn4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_4563 Atcc 4563]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PN4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PN4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1pn4]] 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=1PN4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PN4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HDC:3R-HYDROXYDECANOYL-COENZYME+A'>HDC</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]] 2.35Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pn2|1pn2]]</td></tr> | + | <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=HDC:3R-HYDROXYDECANOYL-COENZYME+A'>HDC</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FOX2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5482 ATCC 4563])</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=1pn4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pn4 OCA], [https://pdbe.org/1pn4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pn4 RCSB], [https://www.ebi.ac.uk/pdbsum/1pn4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pn4 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=1pn4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pn4 OCA], [http://pdbe.org/1pn4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pn4 RCSB], [http://www.ebi.ac.uk/pdbsum/1pn4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pn4 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 4563]] | + | [[Category: Candida tropicalis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Glumoff, T]] | + | [[Category: Glumoff T]] |
| - | [[Category: Haapalainen, A M]] | + | [[Category: Haapalainen AM]] |
| - | [[Category: Hiltunen, J K]] | + | [[Category: Hiltunen JK]] |
| - | [[Category: Koski, M K]] | + | [[Category: Koski MK]] |
| - | [[Category: Enzyme-product complex]]
| + | |
| - | [[Category: Hot-dog fold]]
| + | |
| - | [[Category: Hydratase 2 motif]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Oxyanion hole]]
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| Structural highlights
Function
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.
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 PubMed
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 <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.
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:15051722[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Koski MK, Haapalainen AM, Hiltunen JK, Glumoff T. A two-domain structure of one subunit explains unique features of eukaryotic hydratase 2. J Biol Chem. 2004 Jun 4;279(23):24666-72. Epub 2004 Mar 29. PMID:15051722 doi:10.1074/jbc.M400293200
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