TY - JOUR
T1 - Structural basis for backbone N-methylation by an interrupted adenylation domain
AU - Mori, Shogo
AU - Pang, Allan H.
AU - Lundy, Taylor A.
AU - Garzan, Atefeh
AU - Tsodikov, Oleg V.
AU - Garneau-Tsodikova, Sylvie
N1 - Publisher Copyright:
© 2018 Nature America Inc., part of Springer Nature. All rights reserved.
PY - 2018/5/1
Y1 - 2018/5/1
N2 - 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.
AB - 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.
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U2 - 10.1038/s41589-018-0014-7
DO - 10.1038/s41589-018-0014-7
M3 - Article
C2 - 29556104
AN - SCOPUS:85044216044
SN - 1552-4450
VL - 14
SP - 428
EP - 430
JO - Nature Chemical Biology
JF - Nature Chemical Biology
IS - 5
ER -