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TitleIterative acylation on mature lasso peptides by widespread acetyltransferases.
Journal, issue, pagesNat Chem Biol, Year 2026
Publish dateMar 13, 2026
AuthorsJiang Xiong / Shanquan Wu / Zi-Qi Liang / Shuo Fang / Fen-Yu Tao / Xiao-Tong Gong / Xing Wu / Qingfeng Wu / Jiao-Jiao Cui / Kun Gao / Kin Kuan Hoi / Yong Peng / Shangwen Luo / Dongsheng Lei / Shi-Hui Dong /
PubMed AbstractThe biosynthesis of ribosomally synthesized and posttranslationally modified peptides (RiPPs) leverages iterative catalysis to enhance structural and biological diversity. Traditionally, iterative ...The biosynthesis of ribosomally synthesized and posttranslationally modified peptides (RiPPs) leverages iterative catalysis to enhance structural and biological diversity. Traditionally, iterative enzymes install posttranslational modifications on linear peptides, rather than mature RiPPs with intricate three-dimensional structures, which require complex changes in substrate binding. Here we present a prolific class of GCN5-related N-acetyltransferases (GNATs) that iteratively and consecutively acylate two Lys residues within the loop and ring motifs of lasso peptides, diverging from the typical iterative modification of linear peptides. Utilizing high-resolution cryogenic-electron microscopy and enzymatic reconstitution, we define the lasso peptide-binding pocket of IatT and pinpoint key residues that distinguish its two distinct acetylation steps. Structure-based engineering of IatT's acetyl-recognition site expands the cavity to accommodate longer-chain acyl groups, enabling the creation of lipolasso peptides, a class of ribosomal lipopeptide. This engineering strategy can be applied to any RiPP biosynthetic gene cluster encoding GNAT, facilitating the efficient diversification of ribosomal lipopeptides.
External linksNat Chem Biol / PubMed:41826761
MethodsEM (single particle)
Resolution2.0 - 3.43 Å
Structure data

60983

9iy3

EMDB-60983, PDB-9iy3:
Iterative acetyltransferase on lasso peptides from Actinomycetes in complex with CoA
Method: EM (single particle) / Resolution: 2.17 Å

60984

9iy4

EMDB-60984, PDB-9iy4:
Iterative acetyltransferase on lasso peptides from Actinomycetes in complex with AcCoA
Method: EM (single particle) / Resolution: 2.0 Å

64004

9ubc

EMDB-64004, PDB-9ubc:
Sub-particle structure of the iterative acetyltransferase from Actinomycetes in complex with AcCoA and monoacetylated lasso peptides
Method: EM (single particle) / Resolution: 3.43 Å

Chemicals

ChemComp-COA:
COENZYME A

ChemComp-ACO:
ACETYL COENZYME *A

Source
  • actinosynnema mirum dsm 43827 (bacteria)
  • Actinomycetes (high G+C Gram-positive bacteria)
  • actinosynnema mirum (strain atcc 29888 / dsm 43827 / jcm 3225 / nbrc 14064 / ncimb 13271 / nrrl b-12336 / imru 3971 / 101) (bacteria)
KeywordsTRANSFERASE / GCN5-related N-acetyltransferases / Actinomycetes / CoA / AcCoA / Lasso peptides

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