5L82

NMR Structure of Enterocin K1 in 50%/50% TFE/Water

Summary for 5L82

• Entry DOI: 10.2210/pdb5l82/pdb
• NMR Information: BMRB: 34006
• Descriptor: Enterococcin K1 (1 entity in total)
• Functional Keywords: structure from cyana 2.1, unknown function, antibiotic, membrane interacting, bacteriocin, entk1
• Biological source: Enterococcus faecium EnGen0026
• Total number of polymer chains: 1
• Total formula weight: 4572.40

Authors

Ovchinnikov, K.,Kristiansen, P.E.,Diep, D. (deposition date: 2016-06-06, release date: 2017-05-17, Last modification date: 2024-06-19)

Primary citation

Ovchinnikov, K.V.,Kristiansen, P.E.,Straume, D.,Jensen, M.S.,Aleksandrzak-Piekarczyk, T.,Nes, I.F.,Diep, D.B.
The Leaderless Bacteriocin Enterocin K1 Is Highly Potent against Enterococcus faecium: A Study on Structure, Target Spectrum and Receptor.
Front Microbiol, 8:774-774, 2017

PubMed Abstract: Enterocin K1 (EntK1), enterocin EJ97 (EntEJ97), and LsbB are three sequence related leaderless bacteriocins. Yet LsbB kills only lactococci while EntK1 and EntEJ97 target wider spectra with EntK1 being particularly active against , including nosocomial multidrug resistant isolates. NMR study of EntK1 showed that it had a structure very similar to LsbB - both having an amphiphilic N-terminal α-helix and an unstructured C-terminus. The α-helix in EntK1 is, however, about 3-4 residues longer than that of LsbB. Enterococcal mutants highly resistant to EntEJ97 and EntK1 were found to have mutations within , a gene encoding a stress response membrane-bound Zn-dependent protease. Heterologous expression of the enterococcal rendered resistant cells of sensitive to EntK1 and EntEJ97, suggesting that RseP likely serves as the receptor for EntK1 and EntEJ97. It was also shown that the conserved proteolytic active site in RseP is partly required for EntK1 and EntEJ97 activity, since alanine substitutions of its conserved residues (HExxH) reduced the sensitivity of the clones to the bacteriocins. RseP is known to be involved in bacterial stress response. As expected, the growth of resistant mutants with mutations within was severely affected when they were exposed to higher (stressing) growth temperatures, e.g., at 45°C, at which wild type cells still grew well. These findings allow us to design a hurdle strategy with a combination of the bacteriocin(s) and higher temperature that effectively kills bacteriocin sensitive bacteria and prevents the development of resistant cells.

PubMed: 28515717
DOI: 10.3389/fmicb.2017.00774

Experimental method

SOLUTION NMR