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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology Communications, 6(71), p. 671-675, 2015

DOI: 10.1107/s2053230x15006226

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Overexpression, purification, crystallization and preliminary X-ray diffraction of the nisin resistance protein fromStreptococcus agalactiae

Journal article published in 2015 by Sakshi Khosa, Astrid Hoeppner ORCID, Diana Kleinschrodt, Sander H. J. Smits
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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Data provided by SHERPA/RoMEO

Abstract

Nisin is a 34-amino-acid antimicrobial peptide produced byLactococcus lactisbelonging to the class of lantibiotics. Nisin displays a high bactericidal activity against various Gram-positive bacteria, including some human-pathogenic strains. However, there are some nisin-non-producing strains that are naturally resistant owing to the presence of thensrgene within their genome. The encoded protein, NSR, cleaves off the last six amino acids of nisin, thereby reducing its bactericidal efficacy. An expression and purification protocol has been established for the NSR protein fromStreptococcus agalactiaeCOH1. The protein was successfully crystallized using the vapour-diffusion method in hanging and sitting drops, resulting in crystals that diffracted X-rays to 2.8 and 2.2 Å, respectively.