7lth | pdb_00007lth

Structure of the alpha-N-methyltransferase (SonM mutant Y93F) and RiPP precursor (SonA) heteromeric complex (no cofactor)

spinqualitylabelsall models 7lth, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7lth is a 4 chain structure with sequence from Shewanella oneidensis MR-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: IML, MLE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8EGW3_SHEON Publication Abstract from PubMed Peptide backbone alpha-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 alpha-N-methylations on translated peptides. Here we report the discovery of type IV borosin natural product pathways (termed 'split borosins'), featuring an iteratively acting alpha-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 alpha-N-methyltransferase and substrate. Along with mutational and kinetic analyses, our results give rare context into potential strategies for iterative maturation of RiPPs. Conformational rearrangements enable iterative backbone N-methylation in RiPP biosynthesis.,Miller FS, Crone KK, Jensen MR, Shaw S, Harcombe WR, Elias MH, Freeman MF Nat Commun. 2021 Sep 9;12(1):5355. doi: 10.1038/s41467-021-25575-7. PMID:34504067 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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