7rc6

Aeronamide N-methyltransferase, AerE, bound to modified peptide substrate, AerA-DL,34

spinqualitylabelsall models 7rc6, resolution 1.71Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7rc6 is a 2 chain structure with sequence from Microvirgula aerodenitrificans DSM 15089. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.71Å Ligands: DAL, DLE, DSG, DTH, DVA, NA, SAH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A2S0PEL5_9NEIS Publication Abstract from PubMed 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. Structure and mechanism for iterative amide N-methylation in the biosynthesis of channel-forming peptide cytotoxins.,Cogan DP, Bhushan A, Reyes R, Zhu L, Piel J, Nair SK Proc Natl Acad Sci U S A. 2022 Mar 29;119(13):e2116578119. doi:, 10.1073/pnas.2116578119. Epub 2022 Mar 22. PMID:35316135 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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