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Structures of the DfsB Protein Family Suggest a Cationic, Helical Sibling Lethal Factor Peptide

DOI: 10.1016/j.jmb.2016.01.013 DOI Help
PMID: 26804569 PMID Help

Authors: Jonathan Taylor (Imperial College London) , Gabrielle Taylor (Imperial College London) , Stephen A. Hare (Imperial College London) , Steve Matthews (Imperial College London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Molecular Biology

State: Published (Approved)
Published: January 2016

Open Access Open Access

Abstract: Bacteria have developed a variety of mechanisms for surviving harsh environmental conditions, nutrient stress and overpopulation. Paenibacillus dendritiformis produces a lethal protein (Slf) that is able to induce cell death in neighbouring colonies and a phenotypic switch in more distant ones. Slf is derived from the secreted precursor protein, DfsB, after proteolytic processing. Here, we present new crystal structures of DfsB homologues from a variety of bacterial species and a surprising version present in the yeast Saccharomyces cerevisiae. Adopting a four-helix bundle decorated with a further three short helices within intervening loops, DfsB belongs to a non-enzymatic class of the DinB fold. The structure suggests that the biologically active Slf fragment may possess a C-terminal helix rich in basic and aromatic residues that suggest a functional mechanism akin to that for cationic antimicrobial peptides.

Journal Keywords: X-ray detected ferromagnetic resonance; Spin pumping; Spintronics; Topological insulators

Subject Areas: Biology and Bio-materials

Instruments: I03-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography