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 necessity of studying extremophile organisms is exemplified by the structure of photosystem I from a high-light tolerant cyanobacteria, demonstrating the relationship between the structure and function in photosystem I.
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.
