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π-stacking interactions unique between residues of PUMA and Bcl-xL, which lead to the unfolding of Bcl-xL via an allosteric mechanism, are required to disrupt p53–Bcl-xL interaction and induce apoptosis. This is the first example of regulated protein unfolding for signal transmission.
Heterologous expression of the two components of enterococcal cytolysin with a lanthionine synthetase enables the structural determination of this antimicrobial and hemolytic pair, revealing unexpected stereochemistry in one of the lanthionine bridges that is driven by peptide sequence.
A natural aliphatic alcohol ligand of the mouse orphan odorant receptor Olfr288 from the male preputial gland is regulated by testosterone and affects attractiveness to female mice.
Ubiquitin-conjugating (E2) enzymes contain a conserved asparagine that has been proposed to stabilize an oxyanion intermediate. Structural and biochemical studies of Ubc13 suggest that this residue has a structural role in stabilizing the E2 active site.
Methylation of lysine residues regulates chromatin function in part by recruiting readers to these marks. UNC1215, a selective antagonist of the methyllysine reader L3MBTL3 with a polyvalent mode of interaction, reveals BCLAF1 as a methyllysine-dependent interaction partner for L3MBTL3.
