Structure-function analyses reveal the mechanistic underpinnings of inside-out transmembrane signaling that controls periplasmic proteolysis, and thereby biofilm formation, in bacteria and may be relevant in the context of other signaling proteins with similar control elements.

LAP1 adopts an AAA+ like fold that, while unable to bind nucleotide, can enhance ATPase activity in the neighboring TorsinA protomer in an unusual heterohexameric ring, via an arginine finger.

A combination of light and electron microscopy data provide new insights into the dynamic architecture and the function of the endocytic protein machinery in relation to membrane shape changes in vivo.

Daple is a guanine nucleotide-exchange factor (GEF) for trimeric G proteins that enables Wnt/Frizzled receptors to transactivate G proteins during non-canonical Wnt signaling.

A phage-encoded protein inhibits a bacterial replicative helicase loading factor by exploiting an internal site that auto-regulates loader self-assembly and ATPase activity.

Crystal structures of Nanos bound to Pumilio and target RNAs demonstrate how Nanos forms a molecular clamp to alter Pumilio RNA regulation and specificity in embryonic development and germline maintenance.

A structural study reveals how the simian virus 40 Large-T hexamer helicase interacts with its origin DNA and partially melts the origin double-stranded DNA within the hexamer channel.

Using GPUs for the costly computations in cryo-EM enables structure determination in mere days on a single workstation.

The structure of the promising malaria blood-stage vaccine candidate antigen PfCyRPA and the characterization of a protective epitope are facilitating research on its essential role in parasite invasion, and will guide future epitope-focused vaccine design.

An unbiased chemical screen identifies the AAA+ membrane metalloprotease FtsH1 as a novel apicoplast biogenesis factor and druggable antimalarial target.