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.
Structural and biochemical studies indicate that AAA+ ATPase employ a general mechanism to translocate a variety of substrates, including extended polypeptides, hairpins, crosslinked chains, and chains conjugated to other molecules.
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.
The motor protein kinesin utilizes its fuel molecule by active and concerted motions of its subdomains, while it rapidly interacts with the microtubule track by forming a wet and dynamic interface.
High resolution SthK channel cryo-EM structures in different ligand-bound states combined with single-channel functional data in the same conditions constrain a gating mechanism for CNG channels.