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

Shogo Mori, Allan H. Pang, Taylor A. Lundy, Atefeh Garzan, Oleg V. Tsodikov, Sylvie Garneau-Tsodikova

Research output: Contribution to journalArticlepeer-review

28 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)428-430
Number of pages3
JournalNature Chemical Biology
Volume14
Issue number5
DOIs
StatePublished - May 1 2018
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Structural basis for backbone N-methylation by an interrupted adenylation domain'. Together they form a unique fingerprint.

Cite this