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7LTH

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

Summary for 7LTH
Entry DOI10.2210/pdb7lth/pdb
Related7LTC 7LTE 7LTF
DescriptorTP-methylase family protein, LigA domain-containing protein (3 entities in total)
Functional Keywordsposttranslational modifications; ribosomally synthesized and posttranslationally modified peptides; alpha-n-methyltransferase; borosin; sam, transferase
Biological sourceShewanella oneidensis
More
Total number of polymer chains4
Total formula weight73805.96
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 citationMiller, 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: 34504067
DOI: 10.1038/s41467-021-25575-7
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

226707

數據於2024-10-30公開中

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