Malhar Patel

Malhar Patel

Induced Alpha Helix Formation During Biosynthesis of Microviridins

Authors

Malhar Patel, Garret M. Rubin, Yousong Ding, PhD

Mentor

Yousong Ding

College

College of Pharmacy

Abstract

Microviridins are bioactive tricyclic peptides belonging to a group of ribosomally-synthesized and post-translationally modified peptides (RiPPs), with potent activity as serine protease inhibitors. Microviridins have a minimal biosynthetic gene cluster of a precursor peptide and two ATP-grasp enzymes. The ATP-grasp enzymes recognized a conserved recognition element in the N-terminal leader region of the precursor peptide, which activates the enzymes and enable modification of the peptide substrate. The leader motif, PFFARFL, is a highly conserved region that is induced into an α-helical structure which is essential for interaction with the first ATP-grasp enzyme, MdnC. In order to understand how microviridin and microviridin-like precursors are modified, it is essential to understand the residues that are required for the α-helical structure recognition site. This work explores the conservation of an α-helix motif in microviridin peptides and binding requirements through bioinformatics efforts, including genome mining, sequence alignments and network mapping, and structural prediction. We found that the predicted α-helical regions were at sites that had highly conserved proline and lysine residues. This data indicated that these residues are essential for the induction of the leader motif into an α-helical structure.

Poster

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