| Literature DB >> 33315009 |
Jack Alfred Bryant1, Faye C Morris1, Timothy J Knowles1,2, Michael Overduin2,3, Ian R Henderson1,4, Riyaz Maderbocus1,5, Eva Heinz6, Gabriela Boelter1, Dema Alodaini1, Adam Colyer1, Peter J Wotherspoon1, Kara A Staunton1, Mark Jeeves5, Douglas F Browning1, Yanina R Sevastsyanovich1, Timothy J Wells1, Amanda E Rossiter1, Vassiliy N Bavro1, Pooja Sridhar2, Douglas G Ward2, Zhi-Soon Chong4, Emily Ca Goodall1,7, Christopher Icke1,7, Alvin Ck Teo8, Shu-Sin Chng4,8, David I Roper8, Trevor Lithgow6, Adam F Cunningham1,9, Manuel Banzhaf1.
Abstract
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 and function. Here, we reveal DolP is a lipoprotein functionally conserved amongst Gram-negative bacteria and that loss of DolP increases membrane fluidity. We present the NMR solution structure for Escherichia coli DolP, which is composed of two BON domains that form an interconnected opposing pair. The C-terminal BON domain binds anionic phospholipids through an extensive membrane:protein interface. This interaction is essential for DolP function and is required for sub-cellular localisation of the protein to the cell division site, providing evidence of subcellular localisation of these phospholipids within the outer membrane. The structure of DolP provides a new target for developing therapies that disrupt the integrity of the bacterial cell envelope.Entities:
Keywords: BON domain; E. coli; Escherichia coli; YraP; biochemistry; cell division; chemical biology; infectious disease; microbiology; phospholipids
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Year: 2020 PMID： 33315009 PMCID： PMC7806268 DOI： 10.7554/eLife.62614
Source DB: PubMed Journal: Elife ISSN： 2050-084X Impact factor: 8.140