The first structure of a bacteriophage-encoded S-adenosyl methionine degrading enzyme was solved and demonstrated to catalyze a unimolecular lyase reaction occurring at the domain interface of a trimeric structure.
Electrophysiological and structural characterizations reveal that a previously proposed ion channel responsible for sensing mechanical pain is insensitive to poking or stretching stimuli for conducting ions and may serve as a coenzyme A-binding protein instead.
An integrated biochemical and evolutionary analysis shows how enzyme specificity evolves after gene loss during genome decay, implicating relaxation of purifying selection as a driving force for functional divergence.
The conformations of the enzyme cyclophilin A that are essential for its catalytic activity are temperature dependent and exhibit diverse responses, which is consistent with a complex energy landscape.
A newfound signaling enzyme that diverged from a protein family ubiquitous in bacteria provides mechanistic insights into how new signaling activity emerges to control distinct cellular function and physiology.