Steric complementarity directs sequence promiscuous leader binding in RiPP biosynthesis | Zendy

Jonathan R. Chekan | Zendy; Chayanid Ongpipattanakul | Zendy; Satish K. Nair | Zendy

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Steric complementarity directs sequence promiscuous leader binding in RiPP biosynthesis

Author(s) -

Jonathan R. Chekan,

Chayanid Ongpipattanakul,

Satish K. Nair

Publication year - 2019

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.1908364116

Subject(s) - peptide , biochemistry , peptide sequence , biosynthesis , sequence (biology) , sequence motif , complementarity (molecular biology) , biology , peptide biosynthesis , binding site , computational biology , enzyme , stereochemistry , chemistry , genetics , gene , ribosome , rna

Significance Enzymes involved in the biosynthesis of peptide natural products may be used as platforms for regioselective and chemoselective modifications. These enzymes can catalyze the same chemical transformation on extremely diverse peptide substrates. Here, we show that recruitment of these modification enzymes to a given substrate is dictated by a minimal number of hydrophobic interactions. Installation of this motif can direct modification on unrelated peptide substrates, and establishes a framework for generating new peptidic compounds with drug-like properties.

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