Bryant, Jack Alfred and Morris, Faye C and Knowles, Timothy J and Maderbocus, Riyaz and Heinz, Eva and Boelter, Gabriela and Alodaini, Dema and Colyer, Adam and Wotherspoon, Peter J and Staunton, Kara A and Jeeves, Mark and Browning, Douglas F and Sevastsyanovich, Yanina R and Wells, Timothy J and Rossiter, Amanda E and Bavro, Vassiliy N and Sridhar, Pooja and Ward, Douglas G and Chong, Zhi-Soon and Goodall, Emily CA and Icke, Christopher and Teo, Alvin and Chng, Shu-Sin and Roper, David I and Lithgow, Trevor and Cunningham, Adam F and Banzhaf, Manuel and Overduin, Michael and Henderson, Ian R (2020) 'Structure of dual-BON domain protein DolP identifies phospholipid binding as a new mechanism for protein localization.' eLife, 9. ISSN 2050-084X

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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 among Gram-negative bacteria and that loss of DolP increases membrane fluidity. We present the NMR solution structure for <i>Escherichia coli</i> 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 localization of the protein to the cell division site, providing evidence of subcellular localization 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.

Item Type:	Article
Divisions:	Faculty of Science and Health > Life Sciences, School of
Depositing User:	Elements
Date Deposited:	04 Jan 2021 10:28
Last Modified:	04 Jan 2021 12:15
URI:	http://repository.essex.ac.uk/id/eprint/29444

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