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ATP synthase synthesizes and hydrolyzes ATP by a unique rotational mechanism. A new study elucidates an important step of the catalytic mechanism, the timing of the release of the reaction product Pi in ATP hydrolysis.
The capability to generate multi-omic data sets raises the issue of resource allocation for data generation versus data curation and integration. The initial experience of researchers shows that the effort required for the latter can be much greater than that for the former.
The antiviral S-acyl-2-mercaptobenzamide thioester ejects an essential coordinated zinc ion from and induces aggregation and dysfunction of the HIV-1 nucleocapsid protein NCp7 via repetitive intracellular enzymatic acyl transfers, dependent on acetyl-CoA.
Protein chaperones help misfolded proteins reach their native state, but the necessarily unstable substrates have complicated the analysis of chaperone function. A stable misfolded luciferase substrate now allows the determination of traditional enzyme parameters for the DnaK system, demonstrating that five cycles of unfolding and release are needed for one successful refolding event.
The ability of constrained mutants of the estrogen receptor ligand-binding domain to dictate different conformations of bound partial agonists indicates that the ability of compounds to stabilize each state determines the degree of agonist activity.
A Xenopus laevis two-reporter screen identifies the antihelminthic drug pyrvinium as an inhibitor of the Wnt/β-catenin signaling pathway that works by activating CK1α, which is likely working at the level of Pygopus, a core transcriptional component of the Wnt pathway.
Structural analysis of protein kinase A had previously focused on static pictures with bound inhibitors. The first analyses of the protein with a substrate peptide identify dynamic hot spots and slow steps in catalysis, pointing toward a model of conformational selection in binding.
A magnetic tweezer system that arrests the rotary ATP synthase F1 at the ATP-hydrolysis step provides an order of events to the chemomechanical cycle involving ADP release before phosphate release upon F1 rotation in ATP-hydrolysis mode.
The identification or development of enzymes with new functions remains a significant challenge. A new strategy uses rationally selected sequences anticipated to serve as functional motifs to search the wealth of available genomic data, successfully yielding 17 (R)-selective amine transaminases.
Some cyclodipeptides are unusual in that their cyclic scaffold is created from activated, amino-acid–loaded tRNA substrates. Structural and biochemical evidence now demonstrates that the enzymes that perform this reaction are homologous to tRNA synthetases and use a covalently bound intermediate.
Purine catabolism is typically thought to yield metabolic waste material. However, bioinformatics analysis, coupled with structural and biochemical investigations, now demonstrates that the central carbons of the purine ring can be recycled into glycine in B. subtilis and other bacteria.
Iron-sulfur (Fe-S) clusters are among nature's simplest and most versatile agents of electron transfer. Remarkably, their biological assembly involves an obligatory electron transfer event. It is now revealed that parallel but distinct electron transfer pathways are separately required for compartment-specific Fe-S protein maturation.
Spider dragline silk is an incredibly tough elastomer, but it is also very elastic. Recent work has demonstrated how the mechanical properties of spider silk and other natural elastomers can be mimicked to produce artificial protein-based fibers with great potential for industrial applications.
Mutually exclusive post-translational modifications of flap endonuclease 1 (FEN1) regulate its binding to proliferating cell nuclear antigen (PCNA) and govern its various modes of DNA interaction during DNA replication and repair.
