The structure suggests that the ribosome alone, even without a nascent chain, is sufficient for lateral opening of Sec61 in a lipid environment, independent of its functional state.
The oligosaccharide layer appears to protect the loops while promoting flexibility and multiple conformations while promoting flexibility and multiple conformations in the outer membrane of E. coli outer membranes.
This study investigates how the hydrophobicity of SSs affects the interaction with the Sec complex at the single-molecule level using optical tweezers, and suggests that the Sec complex may selectively recognize and interact with SSs based on their hydrophobicity.
W. Sánchez, Luka Robeson, Hilda M. Alfaro-Valdés et al.· Biochemical and Biophysical...· 0 citations
Regarded as one of the most complex membrane protein folds, CLCs form a large family of membrane proteins that function as anion channels and secondary active anion/proton transporters. Despite low sequence similarity, available structures are remarkably similar, maintaining the same inverted topology and fold, with su...
Janice L. Robertson· Chemical Reviews· 0 citations
Almost all membrane proteins are inserted or translocated across membranes by the universally conserved Sec translocon. Despite its central role, experimental access to Sec function has remained limited. Here, we present ProSecCO (Protein Secretion in Cell-free via synthetic Operons), which is a cell-free protein synth...
M. Meier, Scott A. Scholz, Leo von Bank et al.· Science Advances· 2 citations
It is becoming increasingly clear that large conformational changes in dimeric arrangements deserve attention, alongside other understudied areas like lipid interactions, nucleotide or N-terminal binding to the dimerization domains, and potential roles of the less described member SLC12A9.
Alexandra Náplavová, P. Nissen, R. K. Flygaard· Journal of Structural Biolog...· 0 citations
It is demonstrated that a minimal peptide spanning residues 1216-1228, which bridges the A- and N-domains in the autoinhibited conformation, is sufficient to inhibit ATPase activity.
Michelle Juknaviciute Laursen, Mathilde Roth, P. Nissen et al.· Journal of Membrane Biology· 1 citation
We use cookies to run the site and, with your consent, for analytics and to show ads.
See our Cookie Policy.