Structural basis for backbone N-methylation by an interrupted adenylation domain

Nat Chem Biol. 2018 May;14(5):428-430. doi: 10.1038/s41589-018-0014-7. Epub 2018 Mar 19.

Abstract

Interrupted adenylation domains are enigmatic fusions, in which one enzyme is inserted into another to form a highly unusual bifunctional enzyme. We present the first crystal structure of an interrupted adenylation domain that reveals a unique embedded methyltransferase. The structure and functional data provide insight into how these enzymes N-methylate amino acid precursors en route to nonribosomal peptides.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adenosine Monophosphate / chemistry
  • Amino Acids / chemistry*
  • Catalysis
  • Catalytic Domain
  • Crystallography, X-Ray
  • Enzymes / chemistry*
  • Escherichia coli / metabolism
  • Imines / chemistry
  • Kinetics
  • Methylation*
  • Peptide Synthases / chemistry
  • Peptides / chemistry*
  • Protein Domains
  • Substrate Specificity
  • Time Factors

Substances

  • Amino Acids
  • Enzymes
  • Imines
  • Peptides
  • Adenosine Monophosphate
  • Peptide Synthases