Insights into the key determinants of membrane protein topology enable the identification of new monotopic folds
Name
elife-40889-v2.pdf
Description
Published version
Size
4.23 MB
Format
Adobe PDF
Checksum (MD5)
57a4fca195cda7eb77fdaea863304ef5
Author(s)
Entova, Sonya
Billod, Jean-Marc
Swiecicki, Jean-Marie
Martín-Santamaría, Sonsoles
Imperiali, Barbara
Date Issued
August 2018
Journal
eLIfe
Publisher
eLife Sciences Publications, Ltd
Citation
Entova, Sonya et al. "Insights into the key determinants of membrane protein topology enable the identification of new monotopic folds." eLIfe 7 (August 2018): e40889 © 2018 The Author(s)
Version
Final published version
Abstract
Monotopic membrane proteins integrate into the lipid bilayer via reentrant hydrophobic domains that enter and exit on a single face of the membrane. Whereas many membrane-spanning proteins have been structurally characterized and transmembrane topologies can be predicted computationally, relatively little is known about the determinants of membrane topology in monotopic proteins. Recently, we reported the X-ray structure determination of PglC, a full-length monotopic membrane protein with phosphoglycosyl transferase (PGT) activity. The definition of this unique structure has prompted in vivo, biochemical, and computational analyses to understand and define key motifs that contribute to the membrane topology and to provide insight into the dynamics of the enzyme in a lipid bilayer environment. Using the new information gained from studies on the PGT superfamily we demonstrate that two motifs exemplify principles of topology determination that can be applied to the identification of reentrant domains among diverse monotopic proteins of interest.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
Creative Commons Attribution 4.0 International license
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DOI of Published Version
https://doi.org/10.7554/elife.40889
