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

Jack Alfred Bryant, Faye C Morris, Timothy J Knowles, Riyaz Maderbocus, Eva Heinz, Gabriela Boelter, Dema Alodaini, Adam Colyer, Peter J Wotherspoon, Kara A Staunton, Mark Jeeves, Douglas F Browning, Yanina R Sevastsyanovich, Timothy J Wells, Amanda E Rossiter, Vassiliy N Bavro, Pooja Sridhar, Douglas G Ward, Zhi-Soon Chong, Emily Ca GoodallChristopher Icke, Alvin Ck Teo, Shu-Sin Chng, David I Roper, Trevor Lithgow, Adam F Cunningham, Manuel Banzhaf, Michael Overduin, Ian R Henderson

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Article numbere62614
Publication statusPublished - 14 Dec 2020

Bibliographical note

© 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.


  • 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


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