Discovery of the structural basis for recognition and uptake of a human precursor for body odour production reveals an important role for bacterial peptide transport and novel routes to prevent its production in humans.
Construction of a first atomic model for an intact bacterial ATP synthase allows for a structural understanding of the roles of individual amino acids in the mechanism of ATP synthesis.
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 a ternary complex of a TonB-dependent transporter containing a signalling domain, bound to siderophore as well as TonB, provides mechanistic insights into siderophore uptake and signalling.
Input from computational models has enabled the detection of allosteric communication that modulates the gating mechanism of a bacterial outer-membrane protein.
Building on previous work (Chatterjee et al., 2014), the mechanism of coincidence detection in bacterial second messenger signaling across membranes is revealed at a molecular level, providing insight into the regulation of a conserved transmembrane receptor.
Unlike other similar enzymes, the antimicrobial enzyme PlyC can interact with and translocate eukaryotic membranes, and then lyse and kill intracellular bacteria.
Structure-based alignment of TRP channels enables comparison of structural changes, ion permeation pathways and ligand-binding sites and reveals over-representation of structures that represent non-conducting states.
