BURP-domain proteins belong to an emerging class of autocatalytic copper-containing proteins that modify themselves after synthesis. Now, a report explains how their structure and metal coordination sphere control the installation of crosslinks within the core peptide, and shows how nature leverages mechanistic paradigms to create diversity.
This is a preview of subscription content, access via your institution
Access options
Access Nature and 54 other Nature Portfolio journals
Get Nature+, our best-value online-access subscription
$29.99 / 30 days
cancel any time
Subscribe to this journal
Receive 12 print issues and online access
$259.00 per year
only $21.58 per issue
Buy this article
- Purchase on SpringerLink
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
References
Hudson, G. A. & Mitchell, D. A. Curr. Opin. Microbiol. 45, 61–69 (2018).
Montalbán-López, M. et al. Nat. Prod. Rep. 38, 130–239 (2021).
Chigumba, D. N. et al. Nat. Chem. Biol. 18, 18–28 (2022).
Mydy, L. et al. Nat. Chem. Biol. https://doi.org/10.1038/s41589-024-01552-1 (2024).
Rush, K. W. et al. J. Am. Chem. Soc. 145, 10167–10177 (2023).
Welch, E. F. et al. J. Inorg. Biochem. 231, 111780 (2022).
Prigge, S. T. et al. Nat. Struct. Biol. 6, 976–983 (1999).
Author information
Authors and Affiliations
Corresponding author
Ethics declarations
Competing interests
The author declares no competing interests.
Rights and permissions
About this article
Cite this article
Blackburn, N.J. Ripping and stitching with copper. Nat Chem Biol 20, 404–405 (2024). https://doi.org/10.1038/s41589-024-01582-9
Published:
Issue Date:
DOI: https://doi.org/10.1038/s41589-024-01582-9