5JBW
Crystal structure of LiuC
Summary for 5JBW
| Entry DOI | 10.2210/pdb5jbw/pdb |
| Descriptor | 3-hydroxybutyryl-CoA dehydratase (2 entities in total) |
| Functional Keywords | dehydratase, isovalerate, myxococcus xanthus, lyase |
| Biological source | Myxococcus xanthus (strain DK 1622) |
| Total number of polymer chains | 1 |
| Total formula weight | 27633.72 |
| Authors | Bock, T.,Reichelt, J.,Mueller, R.,Blankenfeldt, W. (deposition date: 2016-04-14, release date: 2016-06-22, Last modification date: 2024-01-10) |
| Primary citation | 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, 17:1658-1664, 2016 Cited by PubMed Abstract: Myxobacteria are able to produce the important metabolite isovaleryl coenzyme A by a route other than 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 and 1.1 Å of LiuC in the apo form and bound to coenzyme A, 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 employs the typical crotonase acid-base mechanism. In this, Tyr231 and Arg69 are key players in positioning the substrate to enable catalysis. Surprisingly, LiuC shows higher sequence and structural similarity to human MGCH than to bacterial forms, although they convert the same substrate. This study provides structural insights into the alternative isovaleryl coenzyme A biosynthesis pathway and might open a path for biofuel research, as isovaleryl-CoA is a source for isobutene, a precursor for renewable fuels and chemicals. PubMed: 27271456DOI: 10.1002/cbic.201600225 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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