6mpz

Publication Abstract from PubMed

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 A 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.

Insights into AMS/PCAT transporters from biochemical and structural characterization of a double Glycine motif protease.,Bobeica SC, Dong SH, Huo L, Mazo N, McLaughlin MI, Jimenez-Oses G, Nair SK, van der Donk WA Elife. 2019 Jan 14;8. pii: 42305. doi: 10.7554/eLife.42305. PMID:30638446^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.