Dual Mode of Action for Plusbacin A3 in Staphylococcus aureus Article Swipe
YOU?
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· 2017
· Open Access
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· DOI: https://doi.org/10.1021/acs.jpcb.6b11039
We have used C{F}, N{F}, and N{P} rotational-echo double resonance NMR to determine the location and conformation of 19F and 15N double-labeled plusbacin A3 and of double-labeled deslipo-plusbacin A3, each bound to the cell walls of whole cells of Staphyloccocus aureus grown in media containing [1-13C]glycine. The 31P is primarily in wall teichoic acid. Approximately 25% of plusbacin headgroups (the cyclic depsipeptide backbone) are in a closed conformation (N-F separation of 6 Å), while 75% are in a more open conformation (N-F separation of 12 Å). The closed headgroups have no contact with wall teichoic acid, whereas the open headgroups have a strong contact. This places the closed headgroups in hydrophobic regions of the cell wall and the open headgroups in hydrophilic regions. None of the plusbacin tails have contact with the 31P of either wall teichoic acid or the cell membrane and thus are in hydrophobic regions of the cell wall. In addition, both heads and tails of plusbacin A3 have contact with the glycyl 13C incorporated in cell-wall peptidoglycan pentaglycyl bridges and with 13C-labeled purines near the membrane surface. We interpret these results in terms of a dual mode of action for plusbacin A3: first, disruption of the peptidoglycan layer nearest to the membrane surface by closed-conformation plusbacin A3 leading to an inhibition of chain extension by transglycosylation; second, thinning and disruption of the membrane (possibly including disruption of ATP-binding cassette transporters embedded in the membrane) by open-conformation plusbacin A3, thereby leading to release of ATP to the hydrophilic regions of the cell wall and subsequent binding by plusbacin A3.
Related Topics
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1021/acs.jpcb.6b11039
- OA Status
- green
- Cited By
- 19
- References
- 21
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W2581766148
Raw OpenAlex JSON
- OpenAlex ID
-
https://openalex.org/W2581766148Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.1021/acs.jpcb.6b11039Digital Object Identifier
- Title
-
Dual Mode of Action for Plusbacin A3 in Staphylococcus aureusWork title
- Type
-
articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2017Year of publication
- Publication date
-
2017-01-31Full publication date if available
- Authors
-
Robert O’Connor, Manmilan Singh, James D. Chang, Sung Joon Kim, Michael S. VanNieuwenhze, Jacob SchaeferList of authors in order
- Landing page
-
https://doi.org/10.1021/acs.jpcb.6b11039Publisher landing page
- Open access
-
YesWhether a free full text is available
- OA status
-
greenOpen access status per OpenAlex
- OA URL
-
https://www.ncbi.nlm.nih.gov/pmc/articles/5555578Direct OA link when available
- Concepts
-
Teichoic acid, Peptidoglycan, Cell wall, Chemistry, Membrane, Biophysics, Bacterial cell structure, Cell membrane, Lipoteichoic acid, Stereochemistry, Crystallography, Staphylococcus aureus, Biochemistry, Bacteria, Biology, GeneticsTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
19Total citation count in OpenAlex
- Citations by year (recent)
-
2024: 2, 2023: 2, 2022: 4, 2021: 1, 2020: 2Per-year citation counts (last 5 years)
- References (count)
-
21Number of works referenced by this work
- Related works (count)
-
10Other works algorithmically related by OpenAlex
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