The ER membrane protein complex (EMC) facilitates the correct topology of the flavivirus non-structural proteins NS4A and NS4B at the ER membrane critical for viral replication.
Efflux of xenobiotic fluoride from microorganisms occurs through a novel family of ion channels with stringent selectivity for fluoride ion and dual-topology molecular architecture.
Homology of vertebrate skull structures should be based on evolutionary continuity and an appreciation of germ layer origins and inductive signaling in the embryonic head.
Cryo electron microscopy and structure-based mutagenesis reveal that the bacteriophage BPP-1 contains two of the three major recognized viral folds, one of which exhibits a new topology.
Key sequence motifs, defined using the first reported structure of a monotopic membrane protein with a reentrant helix, enable identification of new monotopic membrane protein families previously predicted as membrane spanning.
Coarse-grained modeling reveals a new mechanism for multispanning membrane protein topogenesis, in which misintegrated configurations of the proteins undergo post-translational annealing to reach final, fully integrated multispanning topologies.