Version 1
: Received: 28 October 2024 / Approved: 29 October 2024 / Online: 29 October 2024 (10:46:08 CET)
How to cite:
Sinclair, M.; Tajkhorshid, E. The Role of Protein-Lipid Interactions in Priming the Bacterial Translocon. Preprints2024, 2024102268. https://doi.org/10.20944/preprints202410.2268.v1
Sinclair, M.; Tajkhorshid, E. The Role of Protein-Lipid Interactions in Priming the Bacterial Translocon. Preprints 2024, 2024102268. https://doi.org/10.20944/preprints202410.2268.v1
Sinclair, M.; Tajkhorshid, E. The Role of Protein-Lipid Interactions in Priming the Bacterial Translocon. Preprints2024, 2024102268. https://doi.org/10.20944/preprints202410.2268.v1
APA Style
Sinclair, M., & Tajkhorshid, E. (2024). The Role of Protein-Lipid Interactions in Priming the Bacterial Translocon. Preprints. https://doi.org/10.20944/preprints202410.2268.v1
Chicago/Turabian Style
Sinclair, M. and Emad Tajkhorshid. 2024 "The Role of Protein-Lipid Interactions in Priming the Bacterial Translocon" Preprints. https://doi.org/10.20944/preprints202410.2268.v1
Abstract
Protein-lipid interactions demonstrate important regulatory roles in the function of membrane proteins. Nevertheless, due to the semi-liquid nature and heterogeneity of biological membranes, dissecting the details of such interactions at high resolutions continues to pose a major challenge to experimental biophysical techniques. Computational techniques such as molecular dynamics (MD) offer an alternative approach with both temporally and spatially high resolutions. Here we present an extensive series of MD simulations focused on the inner membrane protein YidC (PDB: 6AL2) from Escherichia coli, a key insertase responsible for the integration and folding of membrane proteins. Notably, we observed rare lipid fenestration events, where lipids fully penetrate the vestibule of YidC, providing new insights into the lipid-mediated regulation of protein insertion mechanisms. Our findings highlight the direct involvement of lipids in modulating the greasy slide of YidC and suggest that lipids enhance the local flexibility of the C1 domain, which is crucial for recruiting substrate peptides. These results contribute to a deeper understanding of how lipid-protein interactions facilitate the functional dynamics of membrane protein insertases, with implications for broader studies of membrane protein biology.
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
