7FEA
PY14 in complex with Col-D
Summary for 7FEA
| Entry DOI | 10.2210/pdb7fea/pdb |
| Descriptor | Acetyl-CoA C-acyltransferase, (6~{R},7~{R},9~{E})-6,7-bis(oxidanyl)hexadeca-9,15-dien-11,13-diynoic acid (3 entities in total) |
| Functional Keywords | acetyl-coa acetyltransferase, transferase |
| Biological source | Massilia sp. YMA4 |
| Total number of polymer chains | 4 |
| Total formula weight | 171534.64 |
| Authors | Lin, C.C.,Ko, T.P.,Huang, K.F.,Yang, Y.L. (deposition date: 2021-07-19, release date: 2022-07-27, Last modification date: 2024-10-09) |
| Primary citation | Lin, C.C.,Hoo, S.Y.,Ma, L.T.,Lin, C.,Huang, K.F.,Ho, Y.N.,Sun, C.H.,Lee, H.J.,Chen, P.Y.,Shu, L.J.,Wang, B.W.,Hsu, W.C.,Ko, T.P.,Yang, Y.L. Integrated omics approach to unveil antifungal bacterial polyynes as acetyl-CoA acetyltransferase inhibitors. Commun Biol, 5:454-454, 2022 Cited by PubMed Abstract: Bacterial polyynes are highly active natural products with a broad spectrum of antimicrobial activities. However, their detailed mechanism of action remains unclear. By integrating comparative genomics, transcriptomics, functional genetics, and metabolomics analysis, we identified a unique polyyne resistance gene, masL (encoding acetyl-CoA acetyltransferase), in the biosynthesis gene cluster of antifungal polyynes (massilin A 1, massilin B 2, collimonin C 3, and collimonin D 4) of Massilia sp. YMA4. Crystallographic analysis indicated that bacterial polyynes serve as covalent inhibitors of acetyl-CoA acetyltransferase. Moreover, we confirmed that the bacterial polyynes disrupted cell membrane integrity and inhibited the cell viability of Candida albicans by targeting ERG10, the homolog of MasL. Thus, this study demonstrated that acetyl-CoA acetyltransferase is a potential target for developing antifungal agents. PubMed: 35551233DOI: 10.1038/s42003-022-03409-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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