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| | <StructureSection load='5jbx' size='340' side='right'caption='[[5jbx]], [[Resolution|resolution]] 1.10Å' scene=''> | | <StructureSection load='5jbx' size='340' side='right'caption='[[5jbx]], [[Resolution|resolution]] 1.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jbx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Myxxd Myxxd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JBX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5JBX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jbx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Myxococcus_xanthus_DK_1622 Myxococcus xanthus DK 1622]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JBX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</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]] 1.1Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">crt, MXAN_3757 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246197 MYXXD])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-hydroxybutyryl-CoA_dehydratase 3-hydroxybutyryl-CoA dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.55 4.2.1.55] </span></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=5jbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jbx OCA], [https://pdbe.org/5jbx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jbx RCSB], [https://www.ebi.ac.uk/pdbsum/5jbx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jbx ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5jbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jbx OCA], [http://pdbe.org/5jbx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jbx RCSB], [http://www.ebi.ac.uk/pdbsum/5jbx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jbx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q1D5Y4_MYXXD Q1D5Y4_MYXXD] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 3-hydroxybutyryl-CoA dehydratase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Myxxd]] | + | [[Category: Myxococcus xanthus DK 1622]] |
| - | [[Category: Blankenfeldt, W]] | + | [[Category: Blankenfeldt W]] |
| - | [[Category: Bock, T]] | + | [[Category: Bock T]] |
| - | [[Category: Mueller, R]] | + | [[Category: Mueller R]] |
| - | [[Category: Reichelt, J]] | + | [[Category: Reichelt J]] |
| - | [[Category: Dehydratase]]
| + | |
| - | [[Category: Isovalerate]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Myxococcus xanthus]]
| + | |
| Structural highlights
Function
Q1D5Y4_MYXXD
Publication Abstract from PubMed
Myxobacteria are able to produce the important metabolite isovaleryl coenzyme A by using an alternative route besides leucine degradation. The first step into this pathway is mediated by LiuC, a member of the 3-methylglutaconyl CoA hydratases (MGCH). Here we present crystal structures refined to 2.05 A and 1.1 A of LiuC in the apo and the coenzyme A bound state, respectively. By using simulated annealing we modeled the enzyme substrate complex and identified residues potentially involved in substrate binding, specificity and catalysis. The dehydration of 3-hydroxy-3-methylglutaconyl CoA to 3-methylglutaconyl CoA catalyzed by LiuC involves Glu112 and Glu132 and likely proceeds via the typical crotonase acid-base mechanism. In this, Tyr231 and Arg69 are key players in positioning the substrate to enable proper catalysis. Surprisingly, LiuC shows higher sequence and structural similarity to human MGCH than to the bacterial form, although they convert the same substrate. This study provides structural insights into the alternative isovaleryl coenzyme A biosynthesis pathway and may open a gate for biofuel research, since isovaleryl CoA is a source for isobutene, a precursor for renewable fuels and chemicals.
The structure of LiuC, a 3-hydroxy-3-methylglutaconyl CoA dehydratase involved in isovaleryl CoA biosynthesis in Myxococcus xanthus, reveals insights into specificity and catalysis.,Bock T, Reichelt J, Muller R, Blankenfeldt W Chembiochem. 2016 Jun 8. doi: 10.1002/cbic.201600225. PMID:27271456[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bock T, Reichelt J, Muller R, Blankenfeldt W. The structure of LiuC, a 3-hydroxy-3-methylglutaconyl CoA dehydratase involved in isovaleryl CoA biosynthesis in Myxococcus xanthus, reveals insights into specificity and catalysis. Chembiochem. 2016 Jun 8. doi: 10.1002/cbic.201600225. PMID:27271456 doi:http://dx.doi.org/10.1002/cbic.201600225
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