7RC6
Aeronamide N-methyltransferase, AerE, bound to modified peptide substrate, AerA-DL,34
Summary for 7RC6
| Entry DOI | 10.2210/pdb7rc6/pdb |
| Descriptor | Methyltransferase family protein, Aeronamide A peptide, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | sam-dependent, peptide cytotoxin, proteusin, biosynthetic protein, transferase-biosynthetic protein complex, transferase/biosynthetic protein |
| Biological source | Microvirgula aerodenitrificans DSM 15089 More |
| Total number of polymer chains | 2 |
| Total formula weight | 45473.30 |
| Authors | Cogan, D.P.,Reyes, R.,Nair, S.K. (deposition date: 2021-07-07, release date: 2022-03-30, Last modification date: 2024-12-25) |
| Primary citation | Cogan, D.P.,Bhushan, A.,Reyes, R.,Zhu, L.,Piel, J.,Nair, S.K. Structure and mechanism for iterative amide N -methylation in the biosynthesis of channel-forming peptide cytotoxins. Proc.Natl.Acad.Sci.USA, 119:e2116578119-e2116578119, 2022 Cited by PubMed Abstract: SignificanceThe channel-forming proteusins are bacterial helical peptides that allow permeation of positively charged ions to influence membrane potential and cellular physiology. We biochemically characterize the effect of two critical posttranslational modifications on the secondary structure of the peptide substrate. We determine how a methyl group can be added to the side chains of D-Asn residues in a peptide substrate and show how flanking residues influence selectivity. These studies should foster the development of small-molecule peptide ion channels as therapeutics. PubMed: 35316135DOI: 10.1073/pnas.2116578119 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.71 Å) |
Structure validation
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