The Library
Structure of dual BON-domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation
Tools
Tools
Tools
(2020) Structure of dual BON-domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation. eLife, 9 . e62614. doi:10.7554/eLife.62614
|
PDF
WRAP-structure-dual-BON-domain-protein-DolP-identifies-phospholipid-binding-new-mechanism-protein-localisation-Roper-2020.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (3380Kb) | Preview |
Official URL: http://dx.doi.org/10.7554/eLife.62614
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.
| Item Type: | Journal Article | ||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Subjects: | Q Science > QD Chemistry Q Science > QP Physiology Q Science > QR Microbiology |
||||||||||||||||||
| Divisions: | Faculty of Science > Life Sciences (2010- ) | ||||||||||||||||||
| Library of Congress Subject Headings (LCSH): | Gram-negative bacteria , Phospholipids, Protein binding, Hydrophobic surfaces | ||||||||||||||||||
| Journal or Publication Title: | eLife | ||||||||||||||||||
| Publisher: | eLife Sciences Publications Ltd. | ||||||||||||||||||
| ISSN: | 2050-084X | ||||||||||||||||||
| Official Date: | 14 December 2020 | ||||||||||||||||||
| Dates: |
|
||||||||||||||||||
| Date of first compliant deposit: | 18 January 2021 | ||||||||||||||||||
| Volume: | 9 | ||||||||||||||||||
| Article Number: | e62614 | ||||||||||||||||||
| DOI: | 10.7554/eLife.62614 | ||||||||||||||||||
| Status: | Peer Reviewed | ||||||||||||||||||
| Publication Status: | Published | ||||||||||||||||||
| Access rights to Published version: | Open Access | ||||||||||||||||||
| RIOXX Funder/Project Grant: |
|
Request changes or add full text files to a record
Repository staff actions (login required)
 |
View Item |
Downloads
Downloads per month over past year
