Bacteria release ATP as part of their attack in sepsis.

Construction of a first atomic model for an intact bacterial ATP synthase allows for a structural understanding of the roles of individual amino acids in the mechanism of ATP synthesis.

Conformation-specific nanobodies enable to capture and solve the first GTP-bound active structure of a bacterial homolog of the Parkinson-associated LRRK2 protein, providing insights into the activation mechanism of these proteins.

Protein heptosyltransferases modify a group of bacterial autotransporters for virulence function and employ a novel structural mechanism for the processive hyperglycosylation of the autotransporter.

The overall energy conversion efficiency is calculated for a bacterial vesicle that harvests solar energy for ATP production on the basis of an atomic-detail structural model.

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.

Reengineering the nucleotide-binding pocket of an extant ATPase to restore ancestral GTPase activity revealed an ATP-dependent intermediate required for function and suggested why the protein evolved to use ATP.

A high-throughput method to profile tyrosine kinases and phosphotyrosine recognition domains reveals new rules for sequence specificity and maps the effects of mutations on the recognition of tyrosine phosphorylation sites.

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.

A model of early postnatal bacterial meningitis in the mouse demonstrates the transcriptome responses of each of the major meningeal cell types and should prove useful in dissecting the pathophysiology of bacterial meningitis in human infants.