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Unlike other amine oxidase-family enzymes, nicotine oxidoreductase (NicA2) reacts very slowly with oxygen, prompting the search for and identification of a cytochrome c protein (CycN) that is responsible for accepting electrons from NicA2 in vivo.
Laboratory evolution of the bacterial transpeptidase sortase A coupled with yeast display selection enables a change of the enzyme’s substrate preference to recognize and covalently label endogenous amyloid-β protein, impeding the protein’s ability to aggregate.
A new DNA data storage technology—data recording in vivo by electrical stimulation (DRIVES)—places CRISPR-based DNA encoding activity under electrochemical control by coupling cellular redox state to CRISPR array gene expression.
Single-molecule FRET of mGluR2 shows that the conformations of the ligand-binding domain and the linked cysteine-rich domain are loosely coupled during ligand-induced activation and defines two pre-active states linking inactive and active states.
Crystal structures of FEM1C in apo and in complex with a C-degron ending with arginine reveal a binding pocket in FEM1C that recognizes C-degrons and the essential role of C-terminal arginine for recognition.
Beginning with a functional site and building a supporting scaffold around it enables the de novo design of proteins with distinct binding motifs for use in biosensors to detect antibody responses and as ligands of synthetic signaling receptors.
Structural characterization of the substrate adapters of the C-degron pathway reveals the selective recognition mode towards substrates with C-terminal arginine by FEM1A/C and FEM1B.