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

  • ,
  • Allan H. Pang
    ,
  • Taylor A. Lundy
    ,
  • Atefeh Garzan
    ,
  • Oleg V. Tsodikov(corresponding author)
    ,
  • Sylvie Garneau-Tsodikova
*Corresponding author for this work
  • University of Kentucky
Scholary Output:
Contribution to journal
Article
Peer-review

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 Information

Output type

Scholary Output:
Contribution to journal
Article
Peer-review

Original language

English (US)

Pages from-to (Number of pages)

Pages 428-430 (3 pages)

Journal (Volume, Issue Number)

Nature Chemical Biology (Volume 14, Issue 5)

Publication milestones

  • Published - 05/01/2018

Publication status

Published - 05/01/2018

ISSN

1552-4450

Publication IDs

  • Scopus: 85044216044
  • PubMed: 29556104

Publication metrics

Metrics

SciVal
FWCI
2.27
SciVal
Author count
6
SciVal
citations
27
SciVal
Paper percentile
95
SciVal
Top percentile
5
Scopus
citations
Fractional count
1
Fractional count
0.17
Fractional count
5
Fractional count
0.83
Fractional count
1
Fractional count
1

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Citation count
50
Captures
56
Mentions
1

Funding Details

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.).
FundersFunding numbers
UK
-
NSF
MCB-1149427, 1149427