Structural and functional characterization of the pore-forming domain of pinholin S(21)68

Pinholin S(21)68 triggers the lytic cycle of bacteriophage φ21 in infected Escherichia coli. Activated transmembrane dimers oligomerize into small holes and uncouple the proton gradient. Transmembrane domain 1 (TMD1) regulates this activity, while TMD2 is postulated to form the actual “pinholes.” Fo...

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Bibliografiske detaljer
Udgivet i:Proc Natl Acad Sci U S A
Main Authors: Steger, Lena M. E., Kohlmeyer, Annika, Wadhwani, Parvesh, Bürck, Jochen, Strandberg, Erik, Reichert, Johannes, Grage, Stephan L., Afonin, Sergii, Kempfer, Marin, Görner, Anne C., Koch, Julia, Walther, Torsten H., Ulrich, Anne S.
Format: Artigo
Sprog:Inglês
Udgivet: National Academy of Sciences 2020
Fag:
Biological Sciences
Online adgang:https://ncbi.nlm.nih.gov/pmc/articles/PMC7703622/
https://ncbi.nlm.nih.gov/pubmed/33154156
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.2007979117
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