Radical SAM Enzyme WprB Catalyzes Uniform Cross-Link Topology between Trp-C5 and Arg-Cγ on the Precursor Peptide
Abujunaid Habib Khan, Jabal Rahmat Haedar, Vic Kiselov, Viktors Romaņuks, Gints Šmits, Stefano Donadio, Chin‐Soon Phan
Abstract
High Resolution Image Download MS PowerPoint Slide Cross-link containing products from ribosomally synthesized and post-translationally modified peptides (RiPPs) are generated by radical SAM enzymes (rSAM). Here, we bioinformatically expanded rSAM enzymes based on the known families StrB, NxxcB, WgkB, RrrB, TqqB and GggB. Through in vivo functional studies in E. coli, the newly identified enzyme WprB from Xenorhabdus sp. psl was found to catalyze formation of a cross-link between Trp-C5 and Arg-Cγ at three WPR motifs on the precursor peptide WprA. This represents the first report of this type of cross-link by rSAM enzymes.
Topics & Concepts
EnzymePeptideBiochemistryChemistryLink (geometry)StereochemistryBiologyTopology (electrical circuits)Computer scienceComputer networkCombinatoricsMathematicsMetalloenzymes and iron-sulfur proteinsRNA and protein synthesis mechanismsClick Chemistry and Applications