The membrane topology of immunity proteins for the two‐peptide bacteriocins carnobacteriocin XY, lactococcin G, and lactococcin MN shows structural diversity-Reference-Cited by-同舟云学术

The membrane topology of immunity proteins for the two‐peptide bacteriocins carnobacteriocin XY, lactococcin G, and lactococcin MN shows structural diversity

Published:2019-10-30 Issue:1 Volume:9 Page:
ISSN:2045-8827
Container-title:MicrobiologyOpen
language:en
Short-container-title:MicrobiologyOpen

Author:

Britton Angelle P.¹,Ende Sarah R.¹,Belkum Marco J.²,Martin‐Visscher Leah A.¹^ORCID

Affiliation:

1. Department of Chemistry The King's University Edmonton AB Canada

2. Department of Chemistry University of Alberta Edmonton AB Canada

Funder

Natural Sciences and Engineering Research Council of Canada

Publisher

Wiley

Subject

Microbiology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/mbo3.957

Reference48 articles.

1. The expanding structural variety among bacteriocins from Gram-positive bacteria

2. Identification and three-dimensional structure of carnobacteriocin XY, a class IIb bacteriocin produced byCarnobacteria

3. Plasmid-associated bacteriocin production by a strain of Carnobacterium piscicola from meat

4. Bacteriocins of lactic acid bacteria: extending the family

5. Charged residues next to transmembrane regions revisited: “Positive-inside rule” is complemented by the “negative inside depletion/outside enrichment rule”

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