Structure of dual-BON domain protein DolP identifies phospholipid binding as a new mechanism for protein localization
Research output: Contribution to journal › Article › peer-review
Colleges, School and Institutes
- University of Birmingham, School of Biosciences, UK
- Institute for Cancer and Genomic Sciences, University of Birmingham, College of Medical and Dental Sciences, Birmingham, B152TT, UK.
- Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC, Australia.
- University of Birmingham Microbiome Treatment Centre, University of Birmingham, Birmingham, United Kingdom; Department of Gastroenterology, University Hospital Birmingham, Birmingham, United Kingdom. Electronic address: firstname.lastname@example.org.
- Institute of Cancer and Genomic Sciences
- Singapore Gastric Cancer Consortium, National University of Singapore, Singapore.
- Queensland University of Technology (QUT), Queensland, Australia.
- University of Warwick Library, University of Warwick
- Centre for Liver Research, Institute of Immunology and Immunotherapy and National Institute of Health Research Inflammation Biomedical Research Centre Birmingham; University of Birmingham; Birmingham United Kingdom
- Alberta Glycomics Centre, University of Alberta, Alberta, Canada
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.
|Publication status||E-pub ahead of print - 14 Dec 2020|