5COM

Crystal structure of Uncharacterized Protein Q187F5 from Clostridium difficile 630

Summary for 5COM

• Entry DOI: 10.2210/pdb5com/pdb
• Descriptor: Putative conjugative transposon protein Tn1549-like, CTn5-Orf2, D(-)-TARTARIC ACID, SODIUM ION, ... (4 entities in total)
• Functional Keywords: duf1706, dfsb, replication, unknown function
• Biological source: Peptoclostridium difficile 630
• Total number of polymer chains: 2
• Total formula weight: 44456.15

Authors

Taylor, J.D.,Taylor, G.,Matthews, S.J. (deposition date: 2015-07-20, release date: 2016-02-03, Last modification date: 2024-11-13)

Primary citation

Taylor, 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

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

Experimental method

X-RAY DIFFRACTION (1.85 Å)