Structural biology has elucidated the mechanism of a configuration-specific enzyme that decouples D-amino acids from the translational machinery and, therefore, is involved in the enforcement of homochirality during protein synthesis.

The first structure of a bacteriophage-encoded S-adenosyl methionine degrading enzyme was solved and demonstrated to catalyze a unimolecular lyase reaction occurring at the domain interface of a trimeric structure.

Integrative structural analyses of human insulin degradingenzyme (IDE) reveal how IDE selectively degrades peptides that form toxicaggregates, which guides IDE-based therapeutic innovations to treat diabetesand Alzheimer's disease.

A newfound signaling enzyme that diverged from a protein family ubiquitous in bacteria provides mechanistic insights into how new signaling activity emerges to control distinct cellular function and physiology.

Insight into the mechanism of DNA synthesis is provided by the crystal structures of DNA polymerase intermediates.

Genetic change among enzyme orthologous with similar phenotypic properties can cause substantial differences in evolutionary response to a new enzyme function in terms of their molecular and fitness outcomes.

Conventional studies have focused on enzymatic residues directly involved in catalysis; dissecting a potential interaction network within which these ‘catalytic residues’ are embedded provides insights fundamental to enzyme function, evolution, and engineering.

Structures of respiratory complex I from the insect and metazoan model system Drosophila melanogaster reveal its close relationships with the mammalian complex and provide a foundation for new approaches to disentangle mechanisms of complex I catalysis and regulation.

Structural and biochemical data suggest a mechanism for the Synaptojanin1-catalysed reaction and the role of mutations in the onset of associated neurological diseases.

Cryo-EM and particle classification techniques reveal how the electron-bifurcating [FeFe] hydrogenase from Thermotoga maritima multimerizes to connect distant active sites and reveal different conformational states that enable catalysis.