Structure of dual BON-domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation

The Gram-negative outer-membrane envelops the bacterium and functions as a permeability barrier against antibiotics, detergents, and environmental stresses. Some virulence factors serve to maintain the integrity of the outer membrane, including DolP (formerly YraP) a protein of unresolved structure...

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Detalles Bibliográficos
Autores principales: Bryant, Jack Alfred, Morris, Faye C, Knowles, Timothy J, Maderbocus, Riyaz, Heinz, Eva, Boelter, Gabriela, Alodaini, Dema, Colyer, Adam, Wotherspoon, Peter J, Staunton, Kara A, Jeeves, Mark, Browning, Douglas F, Sevastsyanovich, Yanina R, Wells, Timothy J, Rossiter, Amanda E, Bavro, Vassiliy N, Sridhar, Pooja, Ward, Douglas G, Chong, Zhi-Soon, Goodall, Emily CA, Icke, Christopher, Teo, Alvin CK, Chng, Shu-Sin, Roper, David I, Lithgow, Trevor, Cunningham, Adam F, Banzhaf, Manuel, Overduin, Michael, Henderson, Ian R
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2020
Materias:
Biochemistry and Chemical Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7806268/
https://www.ncbi.nlm.nih.gov/pubmed/33315009
http://dx.doi.org/10.7554/eLife.62614

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7806268/
https://www.ncbi.nlm.nih.gov/pubmed/33315009
http://dx.doi.org/10.7554/eLife.62614

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