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

doi:10.1038/s41589-018-0014-7

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 journal › Article › peer-review

44 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 language	English (US)
Pages (from-to)	428-430
Number of pages	3
Journal	Nature Chemical Biology
Volume	14
Issue number	5
DOIs	https://doi.org/10.1038/s41589-018-0014-7
State	Published - May 1 2018
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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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.",

author = "Shogo Mori and Pang, {Allan H.} and Lundy, {Taylor A.} and Atefeh Garzan and Tsodikov, {Oleg V.} and Sylvie Garneau-Tsodikova",

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AU - Pang, Allan H.

AU - Lundy, Taylor A.

AU - Garzan, Atefeh

AU - Tsodikov, Oleg V.

AU - Garneau-Tsodikova, Sylvie

N1 - Funding Information: This work was supported by a NSF CAREER Award MCB-1149427 (to S.G.-T.) and by startup funds from the College of Pharmacy at the University of Kentucky (to S.G.-T. and O.V.T.). 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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Structural basis for backbone N-methylation by an interrupted adenylation domain

Abstract

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