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Crystal structure and mutagenic analysis of a bacteriocin immunity protein, Mun-im.

Jeon HJ, Noda M, Matoba Y, Kumagai T, Sugiyama M
Biochem Biophys Res Commun 378 574-8 (2009)
Cited: 8 times
EuropePMC logo PMID: 19061861

Abstract

Bacteriocin-producing lactic acid bacteria (LAB) possess a self-protection factor, which is generally called an immunity protein. In this study, we determine the crystal structure of an immunity protein, designated Mun-im, which was classified into subgroup B immunity proteins for class IIa bacteriocins. The Mun-im protein takes a left-turning antiparallel four-helix bundle structure with the flexible N- and C-terminal parts. Although the amino acid sequences of the subgroup B immunity proteins are distinguished from those of the subgroup A, the core structure of Mun-im is well-superimposed with that of the subgroup A immunity protein, EntA-im, and the C-terminus of both proteins is flexible. However, the C-terminus of Mun-im is obviously shorter than that of the subgroup A. We found through mutagenic study of Mun-im that the C-terminus and the K86 residue on the helix 4 in the immunity protein molecule are important for expression of the immunity activity on the subgroup B immunity proteins.

Articles - 2zrr mentioned but not cited (2)

  1. Computational de novo design of a four-helix bundle protein--DND_4HB. Murphy GS, Sathyamoorthy B, Der BS, Machius MC, Pulavarti SV, Szyperski T, Kuhlman B. Protein Sci 24 434-445 (2015)
  2. Structures and reactivity of Zr(IV) chlorobenzene complexes. Wu F, Dash AK, Jordan RF. J Am Chem Soc 126 15360-15361 (2004)


Articles citing this publication (6)

  1. Characterization of mundticin L, a class IIa anti-Listeria bacteriocin from Enterococcus mundtii CUGF08. Feng G, Guron GK, Churey JJ, Worobo RW. Appl Environ Microbiol 75 5708-5713 (2009)
  2. Immunity to the Staphylococcus aureus leaderless four-peptide bacteriocin aureocin A70 is conferred by AurI, an integral membrane protein. Coelho ML, Coutinho BG, Cabral da Silva Santos O, Nes IF, Bastos Mdo C. Res Microbiol 165 50-59 (2014)
  3. An alternative allosteric regulation mechanism of an acidophilic l-lactate dehydrogenase from Enterococcus mundtii 15-1A. Matoba Y, Miyasako M, Matsuo K, Oda K, Noda M, Higashikawa F, Kumagai T, Sugiyama M. FEBS Open Bio 4 834-847 (2014)
  4. Phenotypic and genomic characterization of a Vibrio parahaemolyticus strain causing disease in Penaeus vannamei provides insights into its niche adaptation and pathogenic mechanism. Zhang X, Sun J, Chen F, Qi H, Chen L, Sung YY, Huang Y, Lv A, Hu X. Microb Genom 7 (2021)
  5. Structural Basis of the Immunity Mechanisms of Pediocin-like Bacteriocins. Zhu L, Zeng J, Wang J. Appl Environ Microbiol 88 e0048122 (2022)
  6. The structure of pyogenecin immunity protein, a novel bacteriocin-like immunity protein from Streptococcus pyogenes. Chang C, Coggill P, Bateman A, Finn RD, Cymborowski M, Otwinowski Z, Minor W, Volkart L, Joachimiak A. BMC Struct Biol 9 75 (2009)


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