Substrate and effector bound structures of a bacterial ribonucleotide reductase reveal the molecular basis by which substrate preference is modulated by a distal site on the enzyme.
Structure-function analyses reveal the mechanistic underpinnings of inside-out transmembrane signaling that controls periplasmic proteolysis, and thereby biofilm formation, in bacteria and may be relevant in the context of other signaling proteins with similar control elements.
Cryo-electron microscopy structures of human ribonucleotide reductase reveal molecular details of substrate selection and allosteric inhibition through assembly of its large subunit into a ring that excludes its small subunit.
A dual-color TIRFM study reveals a new form of inflammatory regulation, in which a lipid kinase and ion channel reciprocally regulate each other to amplify the response to painful stimuli.
The nucleotide sensing ability of IMPDH1 at the Bateman domain is regulated by light-dependent phosphorylation in the retina, to adjust GTP synthesis to illumination conditions.
Two structurally-unrelated regulatory proteins utilize parallel molecular mechanisms to selectively tune calcium and calmodulin feedback of calcium and sodium ion channels and reveals a novel strategy to engineer synthetic channel modulators.
Allostery in an intrinsically disordered domain of glucocorticoid receptor is mediated by opposing thermodynamic signals that are directed through the production of different isoforms.
Allosteric modulation of BK channels, vital for the physiology of nerve, muscle and endocrine cells, is determined by direct coupling between gating ring RCK1 domains and the voltage sensor function.
The first three-dimensional structure of the PI3KC3 complex I, which is involved in autophagy, provides a framework for understanding the allosteric regulation of lipid kinase activity.
