bioRxiv · 10.1101/2020.07.21.213744
Structure of Macrolide Efflux Protein (MefA/E) in Streptococcus pneumoniae: An in silico approach
Abstract
BackgroundMacrolides are one of the commonest antibiotics used to treat bacterial respiratory tract infections. Resistance to this class of antibiotics is on the rise and is mediated by macrolide efflux (MefA/E) protein as one of the mechanisms. Despite its importance, the structure of this protein is not known yet. MethodsThe publicly available MefA/E protein sequence was used to model the structure. Modelling was performed in I-TASSER, and the model was further refined. Its orientation in a membrane was studied using OPM server. Results and conclusionsThe structure of MefA/E resembled that of Major Facilitator Superfamily (MFS) proteins, with 13 transmembrane helices. It had a V-shaped conformation, with the wider part towards the outer membrane layer.
Explore related subjects
Keep this discovery
Explore connections, maps & timelines
Peela, S. C. M., SHARMA, J., Sistla, S.. 2020-07-22. Structure of Macrolide Efflux Protein (MefA/E) in Streptococcus pneumoniae: An in silico approach. https://doi.org/10.1101/2020.07.21.213744
Cite the original work for its findings. Save a collection to share your selection of sources.