4OZK

Crystal structure of Laterosporulin, a broad spectrum leaderless bacteriocin produced by Brevibacillus laterosporus strain GI-9

Summary for 4OZK

• Entry DOI: 10.2210/pdb4ozk/pdb
• Descriptor: Putative bacteriocin (2 entities in total)
• Functional Keywords: bacteriocin, class iid, leaderless, defensin-like, antimicrobial, heat stable, toxin
• Biological source: Brevibacillus laterosporus
• Total number of polymer chains: 1
• Total formula weight: 5625.32

Authors

Vipul, S.,Thakur, K.G. (deposition date: 2014-02-17, release date: 2014-11-12, Last modification date: 2024-10-23)

Primary citation

Singh, P.K.,Solanki, V.,Sharma, S.,Thakur, K.G.,Krishnan, B.,Korpole, S.
The intramolecular disulfide-stapled structure of laterosporulin, a class IId bacteriocin, conceals a human defensin-like structural module.
Febs J., 282:203-214, 2015

PubMed Abstract: The growing emergence of antibiotic-resistant bacteria has led to the exploration of naturally occurring defense peptides as antimicrobials. In this study, we found that laterosporulin (LS), a class IId bacteriocin, effectively kills active and nonmultiplying cells of both Gram-positive and Gram-negative bacteria. Fluorescence and electron microscopy suggest that growth inhibition occurs because of increased membrane permeability. The crystal structure of LS at 2.0 Å resolution reveals an all-β conformation of this peptide, with four β-strands forming a twisted β-sheet. All six intrinsic cysteines are intramolecularly disulfide-bonded, with two disulfides constraining the N terminus of the peptide and the third disulfide crosslinking the extreme C terminus, resulting in the formation of a closed structure. The significance of disulfides in maintaining the in-solution peptide structure was confirmed by CD and fluorescence analyses. Despite a low overall sequence similarity, LS has disulfide connectivity [C(I)-C(V), C(II)-C(IV), and C(III)-C(VI)] like that of β-defensins and a striking architectural similarity with α-defensins. Therefore LS presents a missing link between bacteriocins and mammalian defensins, and is also a potential antimicrobial lead, in particular against nonmultiplying bacteria.

PubMed: 25345978
DOI: 10.1111/febs.13129

Experimental method

X-RAY DIFFRACTION (2.038 Å)