@article{mbs:/content/journal/micro/10.1099/00221287-144-5-1343, author = "Papathanasopoulos, Maria A. and Dykes, Gary A. and Revol-Junelles, Anne-Marie and Delfour, Antoine and von Holy, Alexander and Hastings, John W.", title = "Sequence and structural relationships of leucocins A-, B- and C-TA33a from Leuconostoc mesenteroides TA33a", journal= "Microbiology", year = "1998", volume = "144", number = "5", pages = "1343-1348", doi = "https://doi.org/10.1099/00221287-144-5-1343", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-144-5-1343", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", keywords = "leucocins", keywords = "Leuconostoc mesenteroides", keywords = "circular dichroism", keywords = "secondary structure", keywords = "bacteriocins", abstract = "Amino acid sequences of two of the three bacteriocins from Leuconostoc mesenteroides TA33a were determined and their sequence-structure relationships investigated. Leucocin B-TA33a consists of 31 amino acid residues, with a molecular mass of 3466 Da. Leucocin B-TA33a does not belong to the pediocin family of bacteriocins, but shares 62% homology with mesenterocin 52B. A partial sequence of 36 amino acids of leucocin C-TA33a (4598 Da) was determined. Leucocin C-TA33a belongs to the class II bacteriocins having the consensus YGNGV motif. The third bacteriocin, leucocin A-TA33a, is identical to leucocin A-UAL 187. Circular dichroism spectra of the leucocins in aqueous solution and micellar SDS indicated that they undergo a structural transition when in a membrane-mimicking environment. Theoretical predictions from circular dichroism data suggest that leucocins A-, B- and C-TA33a adopt a β-structure (48%) in membrane-mimicking environments. Sequence alignments and secondary structure predictions for the N-terminus of leucocins A- and C-TA33a predicted that Cys-9 and Cys-14 are connected by a disulfide bridge and form two β-strands.", }