5omo

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==CRYSTAL STRUCTURE OF RAT PEROXISOMAL MULTIFUNCTIONAL ENZYME TYPE-1 (RPMFE1) COMPLEXED WITH WITH 3S-HYDROXY-DECANOYL-COA AND 3-KETO-DECANOYL-COA==
==CRYSTAL STRUCTURE OF RAT PEROXISOMAL MULTIFUNCTIONAL ENZYME TYPE-1 (RPMFE1) COMPLEXED WITH WITH 3S-HYDROXY-DECANOYL-COA AND 3-KETO-DECANOYL-COA==
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<StructureSection load='5omo' size='340' side='right' caption='[[5omo]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
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<StructureSection load='5omo' size='340' side='right'caption='[[5omo]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5omo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5aaj 5aaj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OMO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OMO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5omo]] is a 2 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=5OMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OMO FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HSC:(S)-3-HYDROXYDECANOYL-COA'>HSC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZOZ:3-KETO-DECANOYL-COA'>ZOZ</scene></td></tr>
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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]] 2.49&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5mgb|5mgb]]</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HSC:(S)-3-HYDROXYDECANOYL-COA'>HSC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZOZ:3-KETO-DECANOYL-COA'>ZOZ</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ehhadh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
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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=5omo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5omo OCA], [https://pdbe.org/5omo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5omo RCSB], [https://www.ebi.ac.uk/pdbsum/5omo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5omo ProSAT]</span></td></tr>
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<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=5omo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5omo OCA], [http://pdbe.org/5omo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5omo RCSB], [http://www.ebi.ac.uk/pdbsum/5omo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5omo ProSAT]</span></td></tr>
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</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ECHP_RAT ECHP_RAT]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The peroxisomal multifunctional enzyme type 1 (MFE1) catalyzes two successive reactions in the beta-oxidation cycle: the 2E-enoyl-CoA hydratase (ECH) and NAD(+)-dependent 3S-hydroxyacyl-CoA dehydrogenase (HAD) reactions. MFE1 is a monomeric enzyme that has five domains. The N-terminal part (domains A and B) adopts the crotonase fold and the C-terminal part (domains C, D and E) adopts the HAD fold. A new crystal form of MFE1 has captured a conformation in which both active sites are noncompetent. This structure, at 1.7 A resolution, shows the importance of the interactions between Phe272 in domain B (the linker helix; helix H10 of the crotonase fold) and the beginning of loop 2 (of the crotonase fold) in stabilizing the competent ECH active-site geometry. In addition, protein crystallographic binding studies using optimized crystal-treatment protocols have captured a structure with both the 3-ketodecanoyl-CoA product and NAD(+) bound in the HAD active site, showing the interactions between 3-ketodecanoyl-CoA and residues of the C, D and E domains. Structural comparisons show the importance of domain movements, in particular of the C domain with respect to the D/E domains and of the A domain with respect to the HAD part. These comparisons suggest that the N-terminal part of the linker helix, which interacts tightly with domains A and E, functions as a hinge region for movement of the A domain with respect to the HAD part.
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Crystallographic binding studies of rat peroxisomal multifunctional enzyme type 1 with 3-ketodecanoyl-CoA: capturing active and inactive states of its hydratase and dehydrogenase catalytic sites.,Sridhar S, Schmitz W, Hiltunen JK, Venkatesan R, Bergmann U, Kiema TR, Wierenga RK Acta Crystallogr D Struct Biol. 2020 Dec 1;76(Pt 12):1256-1269. doi:, 10.1107/S2059798320013819. Epub 2020 Nov 24. PMID:33263331<ref>PMID:33263331</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5omo" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Buffalo rat]]
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[[Category: Large Structures]]
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[[Category: Hiltunen, J K]]
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[[Category: Rattus norvegicus]]
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[[Category: Kasaragod, P]]
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[[Category: Hiltunen JK]]
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[[Category: Kiema, T R]]
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[[Category: Kasaragod P]]
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[[Category: Schmitz, W]]
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[[Category: Kiema T-R]]
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[[Category: Wierenga, R K]]
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[[Category: Schmitz W]]
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[[Category: 3-hydroxyacyl-coa- dehydrogenase]]
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[[Category: Wierenga RK]]
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[[Category: 3-keto-decanoyl-coa]]
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[[Category: 3s-hydroxy-decanoyl-coa]]
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[[Category: Beta-oxidation]]
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[[Category: Crotonase]]
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[[Category: Fatty acid]]
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[[Category: Hydratase]]
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[[Category: Mfe1]]
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[[Category: Oxidoreductase]]
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Current revision

CRYSTAL STRUCTURE OF RAT PEROXISOMAL MULTIFUNCTIONAL ENZYME TYPE-1 (RPMFE1) COMPLEXED WITH WITH 3S-HYDROXY-DECANOYL-COA AND 3-KETO-DECANOYL-COA

PDB ID 5omo

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