A structural and functional analysis of the electron transfer complex between a sulfite oxidase and its redox protein partner reveals an elegant compromise between the requirements for fast and efficient electron transfer and reaction specificity.
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 high-resolution x-ray structure of an asymmetrical SeCitS dimer, present in the inward- and outward-facing state, provides a complete mechanism of substrate and ion translocation in a sodium-dependent symporter.
The crystal structure of Norrie Disease Protein in complex with the extracellular cysteine-rich domain of Frizzled4 receptor and sucrose octasulfate reveals binding sites for Frizzled4, low density lipoprotein receptor related protein 5/6, and proteoglycan.
Structures of CysZ show a antiparallel membrane protein with an unanticipated fold and together with functional characterization provide insight into a bacterial sulfate translocating system.
The structure of gp41with its membrane anchors highlights the flexible linkage of the transmembrane regions and the fuson peptides, which generates an asymmetric conformation, a potential target of MPER bNAbs.
NHE1-CaM complexes of multiple stoichiometries regulate cellular Ca2+-dependent NHE1 activity and can contribute to NHE1 dimerization, the latter shown by the NMR structure of CaM linking two NHE1 cytosolic tails.
Structural and biochemical studies indicate that AAA+ ATPase employ a general mechanism to translocate a variety of substrates, including extended polypeptides, hairpins, crosslinked chains, and chains conjugated to other molecules.
Linking deep mutational scanning with engineered transcriptional reporters in human cell lines establishes a generalizable method for exploring pharmacogenomics, structure, and function across broad classes of drug receptors.
