7RC3

Aeronamide N-methyltransferase, AerE (Y137F)

Summary for 7RC3

Entry DOI	10.2210/pdb7rc3/pdb
Descriptor	Methyltransferase family protein, ASPARTIC ACID, TETRAETHYLENE GLYCOL, ... (9 entities in total)
Functional Keywords	sam-dependent, peptide cytotoxin, proteusin, transferase
Biological source	Microvirgula aerodenitrificans DSM 15089
Total number of polymer chains	1
Total formula weight	43221.84
Authors	Cogan, D.P.,Reyes, R.,Nair, S.K. (deposition date: 2021-07-07, release date: 2022-03-30, Last modification date: 2023-10-18)
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: 35316135 DOI: 10.1073/pnas.2116578119 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.53 Å)

Structure validation