7LTE
Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA) heteromeric complex (with SAH)
Summary for 7LTE
| Entry DOI | 10.2210/pdb7lte/pdb |
| Related | 7LTC |
| Descriptor | TP-methylase family protein, LigA domain-containing protein, S-ADENOSYL-L-HOMOCYSTEINE, ... (4 entities in total) |
| Functional Keywords | posttranslational modifications; ribosomally synthesized and posttranslationally modified peptides; alpha-n-methyltransferase; borosin; sam, transferase |
| Biological source | Shewanella oneidensis More |
| Total number of polymer chains | 4 |
| Total formula weight | 74606.78 |
| Authors | Miller, F.S.,Crone, K.K.,Jensen, M.R.,Shaw, S.,Harcombe, W.R.,Elias, M.,Freeman, M.F. (deposition date: 2021-02-19, release date: 2021-09-29, Last modification date: 2024-10-09) |
| Primary citation | Miller, F.S.,Crone, K.K.,Jensen, M.R.,Shaw, S.,Harcombe, W.R.,Elias, M.H.,Freeman, M.F. Conformational rearrangements enable iterative backbone N-methylation in RiPP biosynthesis. Nat Commun, 12:5355-5355, 2021 Cited by PubMed Abstract: Peptide backbone α-N-methylations change the physicochemical properties of amide bonds to provide structural constraints and other favorable characteristics including biological membrane permeability to peptides. Borosin natural product pathways are the only known ribosomally encoded and posttranslationally modified peptides (RiPPs) pathways to incorporate backbone α-N-methylations on translated peptides. Here we report the discovery of type IV borosin natural product pathways (termed 'split borosins'), featuring an iteratively acting α-N-methyltransferase and separate precursor peptide substrate from the metal-respiring bacterium Shewanella oneidensis. A series of enzyme-precursor complexes reveal multiple conformational states for both α-N-methyltransferase and substrate. Along with mutational and kinetic analyses, our results give rare context into potential strategies for iterative maturation of RiPPs. PubMed: 34504067DOI: 10.1038/s41467-021-25575-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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