Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity

Abstract Non-ribosomal peptide synthetases are important enzymes for the assembly of complex natural products. Within these multi-modular lines, condensation domains perform central function chain assembly, typically by forming a bond between two peptidyl carrier protein (PCP)-bound substrates. In this work, we report structural snapshots domain in with an aminoacyl-PCP acceptor substrate. These structures allow identification mechanism that controls access substrates to active site domains. The also us demonstrate sites do not contain distinct pocket select side substrate during but residues within motif can instead serve tune selectivity biosynthetic