At the confluence of ribosomally synthesized peptide modification and radical S-adenosylmethionine (SAM) enzymology [Protein Structure and Folding]

Radical SAM (RS) enzymology has emerged as a major biochemical strategy for the homolytic cleavage of unactivated C-H bonds. At the same time, the posttranslational modification of ribosomally encoded peptides is a rapidly expanding area of investigation, already shown to lead to a wide range of natural products that include a redox cofactor, antibiotics, quorum-sensing molecules, growth regulators, and mature proteins. In this mini-review, we discuss the cross-section of these two disciplines, highlighting the recently uncovered importance of protein-protein interactions, in particular, between the ribosomally-encoded peptide substrate and its chaperone, which functions either as a stand-alone protein or as an N-terminal domain to the Radical SAM enzyme in the peptide modification cascade. The need for further structural and functional work on this class of RS enzymes is emphasized, given the poorly understand roles performed by multiple, auxiliary iron-sulfur clusters and the paucity of protein X-ray structural data for RS enzymes.

from # All Medicine by Alexandros G. Sfakianakis via Alexandros G.Sfakianakis on Inoreader http://ift.tt/2wD7mSc
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