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Marine natural products are often made by symbiotic microbes, but octocorals encode their own terpene cyclases that share features with bacterial versions and produce terpenoid precursors, including the coral-exclusive capnellane scaffold.
The linking of salicylaldehydes to a kinase binding scaffold resulted in the development of reversible, lysine-targeted covalent kinase inhibitors with enhanced residence time.
Type I PRMT inhibition elicits potent antitumor activity associated with increased interferon response and intron-retained dsRNA accumulation, suggesting its potential combination with immune checkpoint inhibitors for cancer treatment.
A modular approach for synthesis of proteoglycan glycoconjugates relies on bioorthogonal glycosylation of alkyne-tagged core proteins with azide-tagged glycosaminoglycans to enable the analysis of their functional roles on mammalian cell surfaces.
Biochemical and structural characterization of the bifunctional lanthipeptide protease EryP enables identification of a regulatory interdomain calcium-binding site and leads to a strategy to engineer related enzymes for enhanced catalytic activity.
A genetically encoded metabolic glycan labeling (GeMGL) method based on an orthogonal engineered enzyme–unnatural sugar pair was developed for cell-type-specific glycan labeling in cells and living mice.
Lechner et al. used an affinity-based chemical proteomics approach to investigate the target landscape of HDAC inhibitors, and identified an extracellular vesicle regulator MBLAC2 as a universal off-target of 24 hydroxamate inhibitors.
Using magnetic tweezers, Choi et al. revealed the asymmetric folding pathway of GLUT3, a human glucose transporter, suggesting the active effect of cells in helping glucose transporters overcome folding challenges when forming channels for sugar molecules.
Engineering the biosynthesis, compartmentalization and recycling of three cofactors enables increased production of caffeic acid and ferulic acid in yeast, suggesting that these strategies could improve metabolic flux to other desirable compounds.
Combining the RNA binding and processing capability of Cas6 proteins with toehold-mediated strand displacement enables the dynamic assembly and disassembly of metabolons to control enzyme function and metabolite synthesis.
Cao et al. develop a chemoproteomic pipeline to identify nascent unannotated alt-proteins and show that cell-cycle-regulated alt-protein MINAS-60 is a checkpoint inhibitor of pre-60S assembly.
Ribofuranose residues are installed on O-antigens of bacterial polysaccharides by a dual-activity enzyme that uses phosphoribosyl-5-phospho-d-ribosyl-α-1-diphosphate as a sugar donor and also catalyzes phosphate hydrolysis.
Cryo-EM analysis of the quinolone transporter NorA in complex with synthetic antigen-binding fragments (Fabs) inspired peptide mimics of the Fabs that inhibit methicillin-resistant Staphylococcus aureus in combination with the antibiotic norfloxacin.
Identification of genes associated with resistance to hundreds of cancer therapeutics enabled the discovery of the serine hydrolases MGLL and CES1 as modifiers of sensitivity to GSK-J4 via direct enzymatic modification.
Chemical proteomics analysis of human gastric cells revealed that infection with the stomach bacterium Helicobacter pylori decreases reactivity of legumain Cys219, which alters legumain processing and promotes xenograft tumor growth.
The use of NMR spectroscopy and development of a cellular BRET KRAS engagement assay revealed that noncovalent ligands can access the switch-II pocket of KRAS hotspot mutants.
Biochemical and structural characterization of a standalone ketosynthase, SalC, reveals that it serves as a critical intramolecular aldolase and β-lactone synthase during biosynthesis of the core of the marine natural product salinosporamide A.
The authors present the crystal structure of the MTR1 ribozyme that transfers the methyl group from O6-methylguanine to an adenine N1 in the target RNA and propose a catalytic mechanism based upon proximity, orientation and general acid catalysis.
The crystal structure of the methyltransferase ribozyme MTR1 reveals a cofactor-binding site reminiscent of purine riboswitches and suggests a catalytic mechanism involving nucleobase protonation, resulting in accelerated methyl transfer rates.
The cryo-EM structure of the Csy–dsDNA–AcrIF5 complex and biochemical analysis revealed that five AcrIF5 molecules bind to one Csy–dsDNA complex, destabilizing the helical bundle domain of Cas8f and preventing recruitment of Cas2/3.