Title | Biosynthesis: Leading the way to RiPPs. |
Publication Type | Journal Article |
Year of Publication | 2015 |
Authors | A Link, J |
Journal | Nat Chem Biol |
Volume | 11 |
Issue | 8 |
Pagination | 551-2 |
Date Published | 2015 Aug |
ISSN | 1552-4469 |
Keywords | Amino Acid Sequence, Bacteria, Bacteriocins, Biological Products, Conserved Sequence, Models, Molecular, Molecular Sequence Data, Peptides, PQQ Cofactor, Protein Processing, Post-Translational, Protein Sorting Signals, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Alignment |
Abstract | <p>Many peptide-based natural products require a leader peptide to reach their final modified form, but identifying general rules for leader peptide interactions have been stymied by the diversity of these molecules. Two papers reporting crystallographic and bioinformatic analysis of these systems now reveal a structurally-conserved domain that mediates leader peptide binding.</p> |
DOI | 10.1038/nchembio.1862 |
Alternate Journal | Nat Chem Biol |
PubMed ID | 26196773 |
PubMed Central ID | PMC4794250 |
Grant List | R01 GM107036 / GM / NIGMS NIH HHS / United States |