8T1S
Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA with QSY deletion) heteromeric complex (bound to SAH)
Summary for 8T1S
| Entry DOI | 10.2210/pdb8t1s/pdb |
| Related | 7LTC 7LTE |
| Descriptor | Alpha-N-methyltransferase, Extradiol ring-cleavage dioxygenase LigAB LigA subunit domain-containing protein, S-ADENOSYL-L-HOMOCYSTEINE, ... (5 entities in total) |
| Functional Keywords | alpha-n-methyltransferase, borosin, natural products., transferase |
| Biological source | Shewanella oneidensis More |
| Total number of polymer chains | 4 |
| Total formula weight | 75545.14 |
| Authors | Crone, K.K.,Jomori, T.,Miller, F.S.,Gralnick, J.,Elias, M.,Freeman, M.F. (deposition date: 2023-06-03, release date: 2023-11-22) |
| Primary citation | Crone, K.K.,Jomori, T.,Miller, F.S.,Gralnick, J.A.,Elias, M.H.,Freeman, M.F. RiPP enzyme heterocomplex structure-guided discovery of a bacterial borosin alpha- N -methylated peptide natural product. Rsc Chem Biol, 4:804-816, 2023 Cited by PubMed Abstract: Amide peptide backbone methylation is a characteristic post-translational modification found in a family of ribosomally synthesized and post-translationally modified peptide natural products (RiPPs) called borosins. Previously, we bioinformatically identified >1500 putative borosin pathways in bacteria; however, none of the pathways were associated with a known secondary metabolite. Through in-depth characterization of a borosin pathway in MR-1, we have now identified a bacterially derived borosin natural product named Shewanellamide A. Borosin identification was facilitated by the creation and analysis of a series of precursor variants and crystallographic interrogation of variant precursor and methyltransferase complexes. Along with assaying two proteases from , probable boundaries for proteolytic maturation of the metabolite were projected and confirmed comparison of knockout and overexpression strains. All in all, the natural product was found to be a 16-mer linear peptide featuring two backbone methylations, establishing Shewanellamide A as one of the few borosin metabolites yet identified, and the first from bacteria. PubMed: 37799586DOI: 10.1039/d3cb00093a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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