Insights into AMS/PCAT transporters from biochemical and structural characterization of a double Glycine motif protease
- University of Illinois at Urbana-Champaign, United States
- Universidad de La Rioja, Spain
Abstract
The secretion of peptides and proteins is essential for survival and ecological adaptation of bacteria. Dual-functional ATP-binding cassette transporters export antimicrobial or quorum signaling peptides in Gram-positive bacteria. Their substrates contain a leader sequence that is excised by an N-terminal peptidase C39 domain at a double Gly motif. We characterized the protease domain (LahT150) of a transporter from a lanthipeptide biosynthetic operon in Lachnospiraceae and demonstrate that this protease can remove the leader peptide from a diverse set of peptides. The 2.0 Å resolution crystal structure of the protease domain in complex with a covalently bound leader peptide demonstrates the basis for substrate recognition across the entire class of such transporters. The structural data also provide a model for understanding the role of leader peptide recognition in the translocation cycle, and the function of degenerate, non-functional C39-like domains (CLD) in substrate recruitment in toxin exporters in Gram-negative bacteria.
Data availability
Diffraction data has been deposited at Protein Data Bank under 6MPZ.
Article and author information
Author details
Gonzalo Jiménez-Osés
Wilfred A van der Donk
Funding
National Institutes of Health (GM058822)
- Wilfred A van der Donk
Ministerio de Economía y Competitividad (CTQ2015-70524-R)
- Gonzalo Jiménez-Osés
National Institutes of Health (GM079038)
- Satish K Nair
Ministerio de Economía y Competitividad (RYC-2013-14706)
- Gonzalo Jiménez-Osés
Universidad de La Rioja (Predoctoral fellowship)
- Nuria Mazo
The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
Copyright
© 2019, Bobeica et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
Metrics
-
- 3,346
- views
-
- 579
- downloads
-
- 78
- citations
Views, downloads and citations are aggregated across all versions of this paper published by eLife.
Download links
A two-part list of links to download the article, or parts of the article, in various formats.
Downloads (link to download the article as PDF)
Open citations (links to open the citations from this article in various online reference manager services)
Cite this article (links to download the citations from this article in formats compatible with various reference manager tools)
Insights into AMS/PCAT transporters from biochemical and structural characterization of a double Glycine motif protease
eLife 8:e42305.
https://doi.org/10.7554/eLife.42305
