Mutational analysis and biochemical experiments suggest that the conserved β-hairpin-like membrane-reentrant loop of RseP - an S2P family intramembrane cleaving protease - helps to discriminate substrates by directly interacting with their transmembrane segments.
ER-stress sensing mechanism of the unfolded protein response sensor/transducer IRE1 is conserved from yeast to mammals, where in mammals, unfolded protein binding to IRE1's ER lumenal domain is coupled to its oligomerization and activation through an allosteric conformational change.
An atomic model of the bacterial chemosensory array obtained through the synthesis of cryo-electron tomography and large-scale molecular-dynamics simulations reveals a new kinase conformation during signaling events.
The structure of the recombination complex responsible for flagellar antigen switching in Salmonella enterica, and the mechanism that regulates the site-specific DNA inversion reaction, have been determined.
Structure-based alignment of TRP channels enables comparison of structural changes, ion permeation pathways and ligand-binding sites and reveals over-representation of structures that represent non-conducting states.
The DNA-bridging efficiency of H-NS, a genome organising and transcription regulatory protein, is modulated by changes in environmental conditions of the cell, which drive a structural rearrangement of the protein.