One characterized member of this family, pneumococcal EJ-1 phage holin (EJh; TC# 1.E.11.1.3), is a hydrophobic peptide of 85 amino acyl residues in length (aas) with 2 putative transmembrane segments (TMSs) displaying lethal inner membrane disruptive activity.[2] The synthetic N-terminal TMS flanked by its N-terminal positively charged residues folds into a transmembrane α-helix that increases the membrane permeability. Oligomeric channels of various sizes form depending on the peptide to lipid ratio. By atomic force microscopy, peptide-induced membrane holes can be seen.[3]
^Diaz, E.; Munthali, M.; Lunsdorf, H.; Holtje, J. V.; Timmis, K. N. (1996-02-01). "The two-step lysis system of pneumococcal bacteriophage EJ-1 is functional in gram-negative bacteria: triggering of the major pneumococcal autolysin in Escherichia coli". Molecular Microbiology. 19 (4): 667–681. doi:10.1046/j.1365-2958.1996.399929.x. ISSN0950-382X. PMID8820638. S2CID22961185.
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