Structural and functional characterization of an unanticipated mode of allosteric activity regulation in ribonucleotide reductases controlled by an ATP-cone in the radical-generating subunit.
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.
The molecular chaperone BIP from the endoplasmic reticulum is fine-tuned postranslationally through the thermodynamic and kinetic alterations in its conformational ensemble of functionally and structurally distinct physiological forms.
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.
The SHIP2 inositol phosphatase is an important upstream regulator of the Akt signaling pathway, which requires a catalytic core formed by the phosphatase domain tightly packed to a C2 domain for its 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.
