Structural highlights
FunctionPublication Abstract from PubMedThe growing emergence of antibiotic-resistant bacteria has led to exploring naturally occurring defense peptides as antimicrobials. In this study, we report that laterosporulin, a class IId bacteriocin, effectively kills active and non-multiplying cells of both Gram-positive and Gram-negative bacteria. Fluorescence and electron microscopy suggest that growth inhibition occurs due to increased membrane permeability. Crystal structure of laterosporulin at 2.0 A resolution reveals an all-beta conformation of this peptide with four beta strands forming a twisted beta-sheet. All the six intrinsic cysteine residues are intramolecularly disulfide bonded with two disulfides constraining the N-terminus of the peptide and the third disulfide crosslinks the extreme C-terminus resulting in the formation of a closed structure. Significance of disulfides in maintaining the in-solution peptide structure was confirmed by the circular dichroism and fluorescence analyses. Despite a low overall sequence similarity, laterosporulin has the disulfide connectivity [CI -CV , CII -CIV , CIII -CVI ] like beta-defensins and a striking architectural similarity with alpha-defensins. Therefore laterosporulin presents a missing link between bacteriocins and mammalian defensins and is also a potential antimicrobial lead, in particular against non-multiplying bacteria. This article is protected by copyright. All rights reserved. Intra-molecular Disulfide-Stapled Structure of Laterosporulin, a Class IId Bacteriocin, Conceals Human Defensin-like Structural Module.,Singh PK, Solanki V, Sharma S, Thakur KG, Krishnan B, Korpole S FEBS J. 2014 Oct 27. doi: 10.1111/febs.13129. PMID:25345978[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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