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Post-translational modifications (PTMs) of lysine side chains are important mediators of protein-protein interactions, particularly in chromatin. Photo-lysine, a diazirine analog of lysine, provides a tool to covalently capture proteins that bind lysine and its PTMs.
Cremeomycin is a diazo-containing natural product. Assignment of the functions of individual enzymes in the gene cluster for cremeomycin biosynthesis reveals a pathway by which Streptomyces cremeus converts L-aspartic acid into the nitrous acid needed for diazotization chemistry.
The biosynthesis of iridoids, a class of bicyclic monoterpenes, features an atypical cyclization reaction catalyzed by iridoid synthase (ISY). Crystallographic and biochemical characterization of ISY from Catharanthus roseus provides insights into the ISY enzymatic mechanism and highlights similarities with the homologous progesterone 5β-reductase.
Structure and functional characterization of BpHep, a heparanase from the invasive pathogenic bacterium Burkholderia pseudomallei, defines its glycosaminoglycan recognition mechanism and its catalytic mechanism as an endo-acting glycoside hydrolase.
Some polyketide synthase pathways include branching modules that insert branched monomers into polyketide products. In vitro reconstitution using swapped domains now shows that the mysterious branching (B) domain and the homologous X domain in these modules have structural rather than catalytic roles.
The combination of a light-activated receptor tyrosine kinase and a fluorescent MAPK/ERK reporter results in the development of an optogenetics-based cell screening method to identify small-molecule inhibitors of RTK signaling.
The identification and characterization of two cytochromes P450 from cabbage establish the biochemical basis for synthesizing brassinin-based phytoalexins, using two different routes of S-heterocyclization to construct these important vegetable compounds.
High-throughput chemical screening identified several groups of compounds that selectively block superoxide production from the outer Q-binding site of mitochondrial complex III and protect against ROS-induced oxidative stress in pancreatic β cells.
Enzyme engineering can yield changes in substrate specificity, but limited options exist when mutations are not causing the desired outcome. Selection of monobodies that bind near, but not at, a galactosidase active site now offers another avenue for altering product profiles.
5-Formylcytosine (5fC), produced by TET-mediated oxidation of 5-methylcytosine, is considered an intermediate in active DNA demethylation. Labeling studies and LC/MS analysis across mouse developmental stages reveals that 5fC modifications are more persistent in the genome and may have other functional roles.
The use of a presumed chemical intermediate in the mechanism of enoyl thioester reductase enables the identification of the long-sought proton donor and the rational redesign of enzyme stereoselectivity.
Post-translational regulation of Cas9 activity may improve the specificity of genomic targeting. A modified version of Cas9 with an insertion of a small molecule–regulated intein allows temporal control of Cas9 activity and reduces off-target activity.
Establishing the existence of a Diels-Alderase—an enzyme that catalyzes a concerted [4 + 2] cycloaddition—is made easier by a crystal structure of SpnF, which, along with computational and biochemical analysis, should enable mechanistic investigations.
Modification of the CRISPR/Cas9 genome editing system by the addition of the light inducible proteins CRY2 and CIBI1 enables blue light–mediated transcription of endogenous genes in mammalian cells.
Membrane sorting of Ras and its isolated lipid anchor is based on membrane curvature, sensed by Ras itself. This helps to explain the previous inability to match in vivo results in vitro in promoting the raftophilic Ras to partition with membrane lipid rafts.
Inhibitors of the PAD4 enzyme that bind the inactive enzyme link this protein deiminase and the resultant arginine-to-citrulline modification to formation of neutrophil extracellular traps, highly decondensed chromatin structures with both host-defense and pathological roles.
The natural product albicidin is known to be a potential antibacterial agent, but its missing structure has stymied further studies. Structural determination and biochemical tests of NRPS domains now identify an unusual p-aminobenzoic acid–based compound.
