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

Tools

Bryant, J. A. and Morris, F. C. and Knowles, T. J. and Maderbocus, R. and Heinz, E. and Boelter, G. and Alodaini, D. and Colyer, A. and Wotherspoon, P. J. and Staunton, K. A. and Jeeves, M. and Browning, D. F. and Sevastsyanovich, Y. R. and Wells, T. J. and Rossiter, A. E. and Bavro, V. N. and Sridhar, P. and Ward, D. G. and Chong, Z. S. and Goodall, E. C.A. and Icke, C. and Teo, A. and Chng, S. S. and Roper, D. I. and Lithgow, T. and Cunningham, A. F. and Banzhaf, M. and Overduin, M. and Henderson, I. R. (2021) Structure of dual-BON domain protein DolP identifies phospholipid binding as a new mechanism for protein localization. eLife, 9. e62614. ISSN 2050-084X (https://doi.org/10.7554/eLife.62614)

[thumbnail of Bryant-etal-elife-Structure-of-dual-BON-domain-protein-DolP-identifies-phospholipid-binding]
Preview
 Text. Filename: Bryant-etal-elife-Structure-of-dual-BON-domain-protein-DolP-identifies-phospholipid-binding.pdf
Final Published Version
License: Creative Commons Attribution 4.0 logo
Download (3MB)| Preview

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 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 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.

ORCID iDs

Bryant, J. A., Morris, F. C., Knowles, T. J., Maderbocus, R., Heinz, E. ORCID logoORCID: https://orcid.org/0000-0003-4413-3756, Boelter, G., Alodaini, D., Colyer, A., Wotherspoon, P. J., Staunton, K. A., Jeeves, M., Browning, D. F., Sevastsyanovich, Y. R., Wells, T. J., Rossiter, A. E., Bavro, V. N., Sridhar, P., Ward, D. G., Chong, Z. S., Goodall, E. C.A., Icke, C., Teo, A., Chng, S. S., Roper, D. I., Lithgow, T., Cunningham, A. F., Banzhaf, M., Overduin, M. and Henderson, I. R.;
  • Item type:Article
    ID code:90691
    Dates:
    Date
    Event
    13 January 2021
    Published
    14 December 2020
    Published Online
    11 December 2020
    Accepted
    Subjects:Science > Microbiology
    Department:UNSPECIFIED
    Depositing user: Pure Administrator
    Date deposited:24 Sep 2024 14:59
    Last modified:02 Dec 2024 09:22
    Related URLs:
    URI:https://strathprints.strath.ac.uk/id/eprint/90691
CORE (COnnecting REpositories)