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| ==Kinetic and structural characterization of the 4-oxalocrotonate tautomerase isozymes from Methylibium petroleiphilum== | | ==Kinetic and structural characterization of the 4-oxalocrotonate tautomerase isozymes from Methylibium petroleiphilum== |
| <StructureSection load='4faz' size='340' side='right' caption='[[4faz]], [[Resolution|resolution]] 1.57Å' scene=''> | | <StructureSection load='4faz' size='340' side='right'caption='[[4faz]], [[Resolution|resolution]] 1.57Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4faz]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Metpp Metpp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FAZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FAZ FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4faz]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylibium_petroleiphilum_PM1 Methylibium petroleiphilum PM1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FAZ FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.57Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fdx|4fdx]]</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mpe_A2265 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=420662 METPP])</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=4faz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4faz OCA], [https://pdbe.org/4faz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4faz RCSB], [https://www.ebi.ac.uk/pdbsum/4faz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4faz 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=4faz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4faz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4faz RCSB], [http://www.ebi.ac.uk/pdbsum/4faz PDBsum]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/A2SI32_METPP A2SI32_METPP] |
| Methylibium petroleiphilum strain PM1 uses various petroleum products including the fuel additive methyl tert-butyl ether and straight chain and aromatic hydrocarbons as sole carbon and energy sources. It has two operons, dmpI and dmpII, that code for the enzymes in a pair of parallel meta-fission pathways. In order to understand the roles of the pathways, the 4-oxalocrotonate tautomerase (4-OT) isozyme from each pathway was characterized. Tautomerase I and tautomerase II have the lowest pairwise sequence identity (35%) among the isozyme pairs in the parallel pathways, and could offer insight into substrate preferences and pathway functions. The kinetic parameters of tautomerase I and tautomerase II were determined using 2-hydroxymuconate and 5-(methyl)-2-hydroxymuconate. Both tautomerase I and tautomerase II process the substrates, but with different efficiencies. Crystal structures were determined for both tautomerase I and tautomerase II, at 1.57 and 1.64A resolution, respectively. The backbones of tautomerase I and tautomerase II are highly similar, but have distinct active site environments. The results, in combination with those for other structurally and kinetically characterized 4-OT isozymes, suggest that tautomerase I catalyzes the tautomerization of both 2-hydroxymuconate and alkyl derivatives, whereas tautomerase II might specialize in other aromatic hydrocarbon metabolites.
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| Structural and kinetic characterization of two 4-oxalocrotonate tautomerases in Methylibium petroleiphilum strain PM1.,Terrell CR, Burks EA, Whitman CP, Hoffman DW Arch Biochem Biophys. 2013 Sep 1;537(1):113-24. doi: 10.1016/j.abb.2013.06.016., Epub 2013 Jul 4. PMID:23831510<ref>PMID:23831510</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Metpp]] | | [[Category: Large Structures]] |
| [[Category: Hoffman, D W]] | | [[Category: Methylibium petroleiphilum PM1]] |
| [[Category: Terrell, C R]] | | [[Category: Hoffman DW]] |
| [[Category: Whitman, C P]] | | [[Category: Terrell CR]] |
| [[Category: Alpha/beta fold]] | | [[Category: Whitman CP]] |
| [[Category: Isomerase]]
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| [[Category: Tautomerase]]
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