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.

There is a strand-based evolutionary mechanism for the diversification of outer membrane proteins, which has implications for how repeat proteins are created and for how outer membrane proteins fold.

Structures of CysZ show a antiparallel membrane protein with an unanticipated fold and together with functional characterization provide insight into a bacterial sulfate translocating system.

Linking the DNA repair template to the Cas9 ribonucleoprotein complex enhances homology-directed repair of the induced DNA double strand break.

Human vitamin K epoxide reductase (VKOR) has a four transmembrane domain topology that supports the use of a homology model, enabling identification of active site residues and human variant impact.

The high-resolution structure of a filamentous flexible plant virus shows that there is structural homology between its coat protein and the nucleoproteins of an unrelated group of enveloped RNA animal viruses.

Multiple biochemical assays show that the topology of CCR5 and possibly other GPCRs may be inverted by ceramide or other sphingolipids through the process of regulated alternative translocation.

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.

Comparative genomics and three-dimensional protein modelling identify homologs of insect chemosensory receptors in unicellular eukaryotes and plants.