A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis
- Submitting institution
-
University of Sussex
- Unit of assessment
- 5 - Biological Sciences
- Output identifier
- 427962_70269
- Type
- D - Journal article
- DOI
-
10.1038/s41467-017-00361-6
- Title of journal
- Nature Communications
- Article number
- a263
- First page
- -
- Volume
- 8
- Issue
- 1
- ISSN
- 2041-1723
- Open access status
- Compliant
- Month of publication
- August
- Year of publication
- 2017
- URL
-
https://doi.org/10.1038/s41467-017-00361-6
- Supplementary information
-
-
- Request cross-referral to
- -
- Output has been delayed by COVID-19
- No
- COVID-19 affected output statement
- -
- Forensic science
- No
- Criminology
- No
- Interdisciplinary
- No
- Number of additional authors
-
17
- Research group(s)
-
-
- Citation count
- 28
- Proposed double-weighted
- No
- Reserve for an output with double weighting
- No
- Additional information
- -
- Author contribution statement
- This work describes the high-resolution structure an outer-membrane secretion system from Pseudomonas and combines the structural data with native mass spectrometry, single-channel electrical recording and molecular simulations to confirm how the structure secretes functional amyloid fibres.
Stephen Hare supervised the first author (Sarah Rouse) and assisted in carrying out the crystallography of the membrane protein to reveal its structure. This included conceiving and planning the experiments, analysing and interpreting the data and contributing to the manuscript overall.
- Non-English
- No
- English abstract
- -