Structural Characterization of the S-glycosylated Bacteriocin ASM1 from <i>Lactobacillus plantarum</i>
In order to protect their environmental niche, most bacteria secret antimicrobial substances designed to target specific bacterial strains that are often closely related to the producer strain. Bacteriocins, small, ribosomally synthesised antimicrobial peptides, comprise a class of such substances a...
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| Language: | English |
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MDPI AG
2020-03-01
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| Series: | Magnetochemistry |
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| Online Access: | https://www.mdpi.com/2312-7481/6/1/16 |
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| author | Alexander K. Goroncy Trevor S. Loo Adrian M. Koolaard Mark L. Patchett Gillian E. Norris |
| author_facet | Alexander K. Goroncy Trevor S. Loo Adrian M. Koolaard Mark L. Patchett Gillian E. Norris |
| author_sort | Alexander K. Goroncy |
| collection | DOAJ |
| description | In order to protect their environmental niche, most bacteria secret antimicrobial substances designed to target specific bacterial strains that are often closely related to the producer strain. Bacteriocins, small, ribosomally synthesised antimicrobial peptides, comprise a class of such substances and can either inhibit (bacteriostatic) or kill (bactericidal) target cells. Glycocins are a class of bacteriocin that are post-translationally modified by one or more carbohydrate moieties that are either β-<i>O</i>-linked to either a serine or threonine and/or β-<i>S</i>-linked to a cysteine. The solution nuclear magnetic resonance structure (NMR) of the glycocin ASM1 (produced by <i>Lactobacillus plantarum</i> A-1), an orthologue of GccF, has been determined. In both structures, the disulfide bonds are essential for activity and restrict the mobility of the N-acetyl-glucosamine (GlcNAc) attached to Ser-18 (O-linked), compared to the much more flexible GlcNAc moiety on Cys-43 (S-linked). Interestingly, despite 88% sequence identity, the helical structure of ASM1 is less pronounced which appears to be consistent with the far ultra-violet circular dichroism (UV CD) spectra. |
| first_indexed | 2024-12-21T04:48:40Z |
| format | Article |
| id | doaj.art-9bf86c9ac2704ae4a091e0a665d06f02 |
| institution | Directory Open Access Journal |
| issn | 2312-7481 |
| language | English |
| last_indexed | 2024-12-21T04:48:40Z |
| publishDate | 2020-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Magnetochemistry |
| spelling | doaj.art-9bf86c9ac2704ae4a091e0a665d06f022022-12-21T19:15:30ZengMDPI AGMagnetochemistry2312-74812020-03-01611610.3390/magnetochemistry6010016magnetochemistry6010016Structural Characterization of the S-glycosylated Bacteriocin ASM1 from <i>Lactobacillus plantarum</i>Alexander K. Goroncy0Trevor S. Loo1Adrian M. Koolaard2Mark L. Patchett3Gillian E. Norris4School of Fundamental Sciences, Massey University, Palmerston North 4442, New ZealandSchool of Fundamental Sciences, Massey University, Palmerston North 4442, New ZealandSchool of Fundamental Sciences, Massey University, Palmerston North 4442, New ZealandSchool of Fundamental Sciences, Massey University, Palmerston North 4442, New ZealandSchool of Fundamental Sciences, Massey University, Palmerston North 4442, New ZealandIn order to protect their environmental niche, most bacteria secret antimicrobial substances designed to target specific bacterial strains that are often closely related to the producer strain. Bacteriocins, small, ribosomally synthesised antimicrobial peptides, comprise a class of such substances and can either inhibit (bacteriostatic) or kill (bactericidal) target cells. Glycocins are a class of bacteriocin that are post-translationally modified by one or more carbohydrate moieties that are either β-<i>O</i>-linked to either a serine or threonine and/or β-<i>S</i>-linked to a cysteine. The solution nuclear magnetic resonance structure (NMR) of the glycocin ASM1 (produced by <i>Lactobacillus plantarum</i> A-1), an orthologue of GccF, has been determined. In both structures, the disulfide bonds are essential for activity and restrict the mobility of the N-acetyl-glucosamine (GlcNAc) attached to Ser-18 (O-linked), compared to the much more flexible GlcNAc moiety on Cys-43 (S-linked). Interestingly, despite 88% sequence identity, the helical structure of ASM1 is less pronounced which appears to be consistent with the far ultra-violet circular dichroism (UV CD) spectra.https://www.mdpi.com/2312-7481/6/1/16nmrcircular dichroismbacteriocinpost-translational modificationss-linked glycosylationo-linked glycosylation |
| spellingShingle | Alexander K. Goroncy Trevor S. Loo Adrian M. Koolaard Mark L. Patchett Gillian E. Norris Structural Characterization of the S-glycosylated Bacteriocin ASM1 from <i>Lactobacillus plantarum</i> Magnetochemistry nmr circular dichroism bacteriocin post-translational modifications s-linked glycosylation o-linked glycosylation |
| title | Structural Characterization of the S-glycosylated Bacteriocin ASM1 from <i>Lactobacillus plantarum</i> |
| title_full | Structural Characterization of the S-glycosylated Bacteriocin ASM1 from <i>Lactobacillus plantarum</i> |
| title_fullStr | Structural Characterization of the S-glycosylated Bacteriocin ASM1 from <i>Lactobacillus plantarum</i> |
| title_full_unstemmed | Structural Characterization of the S-glycosylated Bacteriocin ASM1 from <i>Lactobacillus plantarum</i> |
| title_short | Structural Characterization of the S-glycosylated Bacteriocin ASM1 from <i>Lactobacillus plantarum</i> |
| title_sort | structural characterization of the s glycosylated bacteriocin asm1 from i lactobacillus plantarum i |
| topic | nmr circular dichroism bacteriocin post-translational modifications s-linked glycosylation o-linked glycosylation |
| url | https://www.mdpi.com/2312-7481/6/1/16 |
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