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
- University of Kentucky
Scholary Output:
Contribution to journal
Article
Peer-reviewAbstract
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-reviewOriginal 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
1552-4450Publication 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
Fractional count
1
Fractional count
0.17
Fractional count
5
Fractional count
0.83
Fractional count
1
Fractional count
1
PlumX, opens in new tab
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
