Summary for 6SL9
| Entry DOI | 10.2210/pdb6sl9/pdb |
| Descriptor | Enoyl-CoA hydratase/carnithine racemase, GLYCEROL (3 entities in total) |
| Functional Keywords | phenylacetic acid catabolism, isomerase, tropodithietic acid, crotonase |
| Biological source | Thermus thermophilus JL-18 |
| Total number of polymer chains | 1 |
| Total formula weight | 28132.44 |
| Authors | Saleem-Batcha, R.,Spieker, M.,Teufel, R. (deposition date: 2019-08-19, release date: 2019-12-11, Last modification date: 2024-01-24) |
| Primary citation | Spieker, M.,Saleem-Batcha, R.,Teufel, R. Structural and Mechanistic Basis of an Oxepin-CoA Forming Isomerase in Bacterial Primary and Secondary Metabolism. Acs Chem.Biol., 14:2876-2886, 2019 Cited by PubMed Abstract: Numerous aromatic compounds are aerobically degraded in bacteria via the central intermediate phenylacetic acid (paa). In one of the key steps of this widespread catabolic pathway, 1,2-epoxyphenylacetyl-CoA is converted by PaaG into the heterocyclic oxepin-CoA. PaaG thereby elegantly generates an α,β-unsaturated CoA ester that is predisposed to undergo β-oxidation subsequent to hydrolytic ring-cleavage. Moreover, oxepin-CoA serves as a precursor for secondary metabolites (e.g., tropodithietic acid) that act as antibiotics and quorum-sensing signals. Here we verify that PaaG adopts a second role in aromatic catabolism by converting -3,4-didehydroadipoyl-CoA into -2,3-didehydroadipoyl-CoA and corroborate a Δ,Δ-enoyl-CoA isomerase-like proton shuttling mechanism for both distinct substrates. Biochemical and structural investigations of PaaG reveal active site adaptations to the structurally different substrates and provide detailed insight into catalysis and control of stereospecificity. This work elucidates the mechanism of action of unusual isomerase PaaG and sheds new light on the ubiquitous enoyl-CoA isomerases of the crotonase superfamily. PubMed: 31689071DOI: 10.1021/acschembio.9b00742 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.27 Å) |
Structure validation
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