Structural biology

The authors provide a litmus test for the recognition mechanism of transiently binding proteins based on nuclear magnetic resonance and find a conformational selection binding mechanism through concentration-dependent kinetics of ubiquitin and SH3.

How bacteria sense and respond to nitrogen is a key question in microbial physiology. This work unveils the mechanism by which the central nitrogen metabolic enzyme, glutamine synthetase, directly signals nitrogen availability to the GlnR regulator.

Using X-ray crystallography and nonhomologous end-joining assays, this study reveals structural features within Polλ that provide it with the ability to bridge and stabilize tenuous DNA double-strand break ends, allowing for religation.

Folded proteins are composed of secondary structures, α-helices and β-sheets, that are generally assumed to be stable. Here, the authors combine computational prediction with experimental validation to show that many sequence-diverse NusG protein domains switch completely from α-helix to β-sheet folds.

In this work, the authors report a sophisticated combination of genetic, biophysical, and biochemical analyses to identifies the cycling conformational states of PPM1D. The findings reveal how an allosteric inhibitor locks the protein into a conformationally inactive state, and explain the distribution of PPM1D activating mutations in cancer.