Volume 25 Issue 7, July 2018

Cryo-EM analyses of mitochondrial complex I (NADH:ubiquinone oxidoreductase) isolated from mouse heart allow comparisons between the active and deactive states and provide new mechanistic insights into this important complex.

The structural basis for self-assembly of human SYCP1, the core architectural element of the meiotic synaptonemal complex, reveals an obligate tetrameric structure that assembles into a zipper-like supramolecular lattice.

The crystal structure of human AT₂R binding an angiotensin II analog reveals ‘core’ and ‘extended’ domains within the binding pocket. A signature positively charged motif orients the C terminus of the peptide ligand at the bottom of the binding pocket.

Neural network analyses of ribosome profiling data reveal sequence features that affect translation elongation, which can be manipulated to control protein expression levels in yeast.

Cryo-EM structure of the Salmonella Typhimurium FliP–FliQ–FliR complex identifies this export gate as a core component of the periplasmic portion of the type III secretion system.

Structural and functional dissection of the TIRR–53BP1 complex shows that TIRR acts as a regulatory switch that blocks 53BP1 binding to chromatin to direct DNA repair, and it releases 53BP1 in response to DNA damage by binding RNA.

Crystal structures of the CLC^F proton-coupled fluoride antiporter Eca in two conformations capture two rotamers of the gating glutamate and reveal simultaneous accessibility of F^– and H⁺ ions via separate pathways on opposite sides of the membrane.

Cryo-EM analyses of microtubules in different nucleotide-bound states reveal differences in lateral and longitudinal contacts within the lattice, indicating the structural basis for microtubule catastrophe.

Structures of Cdc48 with heterodimeric cofactor Ufd1–Npl4 reveal the location of Npl4's MPN domain above Cdc48’s central pore, thus suggesting how Npl4 engages with polyubiquitinated substrates and promotes their translocation into the ATPase.

Crystal structures of activated, phosphorylated fly parkin in complex with phosphorylated ubiquitin and human UbcH7 reveal large domain movements enabled by the parkin’s internal linkers. Results also explain some Parkinson’s disease mutations.

Using UbiSite, an antibody-based approach that specifically detects protein lysine and N-terminal ubiquitination, Blagoev and colleagues uncover lack of correlation between changes in protein ubiquitination and abundance upon proteasome inhibition.