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5CIV

Sibling Lethal Factor Precursor - DfsB

Summary for 5CIV
Entry DOI10.2210/pdb5civ/pdb
DescriptorSibling bacteriocin (2 entities in total)
Functional Keywordsbacteriocin, sporulation, duf1706, cell cycle, unknown function
Biological sourcePaenibacillus dendritiformis
Total number of polymer chains1
Total formula weight21868.22
Authors
Taylor, J.D.,Matthews, S.J. (deposition date: 2015-07-13, release date: 2016-02-03, Last modification date: 2024-10-09)
Primary citationTaylor, J.D.,Taylor, G.,Hare, S.A.,Matthews, S.J.
Structures of the DfsB Protein Family Suggest a Cationic, Helical Sibling Lethal Factor Peptide.
J.Mol.Biol., 428:554-560, 2016
Cited by
PubMed 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.
PubMed: 26804569
DOI: 10.1016/j.jmb.2016.01.013
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.384 Å)
Structure validation

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