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

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.

Publication DOI: https://doi.org/10.7554/eLife.62614
Divisions: College of Health & Life Sciences > School of Biosciences
Additional Information: © 2020, Bryant et al. This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.
Uncontrolled Keywords: Anti-Bacterial Agents/metabolism,Bacterial Outer Membrane Proteins/metabolism,Cell Membrane/metabolism,Cell Wall/metabolism,Escherichia coli/metabolism,Escherichia coli Proteins/metabolism,Gram-Negative Bacteria/metabolism,Lipoproteins/metabolism,Protein Transport/physiology,Virulence Factors/metabolism
Publication ISSN: 2050-084X
Last Modified: 27 Jun 2024 11:02
Date Deposited: 14 Jan 2022 13:37
Full Text Link:
Related URLs: https://elifesc ... cles/62614#info (Publisher URL)
PURE Output Type: Article
Published Date: 2020-12-14
Accepted Date: 2020-12-11
Authors: 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 (ORCID Profile 0000-0003-4672-3514)
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

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