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Nucleotide-binding proteins are proteins that bind to nucleotides. For example, kinases bind adenosine triphosphate (ATP) and G proteins bind guanosine triphosphate (GTP). Other nucleotide-binding proteins bind nucleotides such as cyclic adenosine monophosphate (cAMP), cyclic guanosine monophosphate (cGMP) and cytidine triphosphate (CTP).
The detailed process of membrane fusion mediated by dynamin-like GTPase atlastin (ATL) remains unclear. Here, authors reveal the conformational dynamics of ATL coupled with GTP hydrolysis cycle at the single molecule level.
The Fic2 enzyme of the pathogen Coxiella burnetii can act as a bifunctional histone modification enzyme, capable of AMPylation (as monomer) and deAMPylation (as dimer) upon DNA binding by a C-terminal helix-turn-helix domain.
Here the authors use cryogenic electron microscopy to solve the Arabidopsis thaliana Argonaute10–guide RNA complex with and without a target RNA representing a slicing substrate, to provide insights into the slicing mechanism of a eukaryotic Argonaute.
Cryo-EM of human PRPS1 shows the nucleotide-synthesizing enzyme assembling into filaments that accommodate active and inhibited conformations. Engineered and disease mutations reveal that filament assembly stabilizes allosteric sites, enhancing catalytic activity.
SARM1 is a key player in axon degeneration. Here, the authors generate a nanobody, which specifically recognizes the NMN-bound state of SARM1 and helps resolve the SARM1 structure in an intermediate state of activation.
An ABC protein that binds the ribosomal exit site suggests a new mechanism for direct regulation of translation in response to changing ATP levels in the cell.
