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

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48 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
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

Bibliographical note

Publisher Copyright:
© 2018 Nature America Inc., part of Springer Nature. All rights reserved.

Funding

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.).

Funders	Funder number
University of Kentucky
National Science Foundation Arctic Social Science Program	MCB-1149427

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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10.1038/s41589-018-0014-7

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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.",

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AU - Garneau-Tsodikova, Sylvie

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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

Bibliographical note

Funding

ASJC Scopus subject areas

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