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.
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.
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.
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.
Mutations that affect a metabolic network generically exhibit epistasis, which propagates to higher level phenotypes, such as fitness, carrying some information about the network’s topology.
Genetics of a canine transmissible tumour show how the world’s oldest cancer “metastasised” through the global dog population – and captured, maintained and rearranged its mitochondrial DNA along the way.
The physical interaction network encoded in the multi-domain protein native structure handles the trade-off between the fast, stable folding and the efficient, reliable function.
