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Lewis and Lu present an approach using a rhodamine tag and a polarization microscope to follow 10°–16° rotation of an ɑ-helix, corresponding to 3.4- to 8.1-Å translation, from the MthK RCK domain in real time.
The energetics of Ca2+-dependent conformational changes in an RCK domain from MthK are now determined from real-time monitoring, leading to a model that predicts the channel’s open probability behavior.
Cryo-EM structure of the dynein-2 complex (involved in intraflagellar transport, IFT) reveals distinct conformations of the two DHC2 tails within the same assembly, suggesting the mechanisms of autoinhibition and of transport on anterograde IFT trains.
Comprehensive genome-wide analyses of nucleosome occupancy and promoter activity after rapid depletion of chromatin remodelers in Saccharomyces cerevisiae provides insight into remodeler function in transcription initiation via nucleosome positioning.
Identification of SFiNX, a complex of Nxf2–Nxt1, a variant of the mRNA export receptor Nxf1–Nxt1 and the Piwi-associated protein Panoramix, demonstrates an RNA export independent role for Nxf2 in piRNA-guided cotranscriptional transposon silencing.
The fly male germline stem cells undergo asymmetric division, with old histones H3 and H4 preferentially retained in the daughter stem cell. The mechanisms that contribute to this outcome are revealed using super-resolution microscopy and DNA fiber analyses.
A combination of biochemical, single-molecule, and in vivo assays reveals that the UV-DDB complex that removes UV-induced DNA lesions via the nucleotide excision repair pathway also promotes removal of oxidative lesions via base excision repair.
X-ray crystal structures of the full-length TcdB exotoxin of bacterial pathogen Clostridium difficile reveal pH-dependent conformational changes that allow translocation of the toxin from endosomes into the cytosol.
AAA+ ATPase spastin recognizes tubulin polyglutamylated C-terminal tails and severs microtubules. A cryo-EM structure of fly spastin with polyGlu reveals how spastin engages with the substrate, an activity allosterically coupled to nucleotide binding and oligomerization.
O-Mannosylation is an essential protein modification implicated in several diseases. Cryo-EM structures of the yeast mannosyltransferase complex Pmt1–Pmt2 bound to substrates reveal the substrate recognition model and confirm the reaction mechanism.
Cryo-EM structures of the active Cas9–sgRNA–DNA complex in the presence of Mg2+ capture Cas9 in the pre- and postcatalytic states as well as in the product-bound state, and reveal coupled domain motions and interactions between the enzyme and nucleic acids.
Transition metal FRET and Rosetta modeling reveal that the S4 helix in the voltage-sensing domain of the HCN channel moves downward and its carboxy-terminal portion tilts during hyperpolarization activation.
Crystal structure of the tubulin carboxypeptidase complex between vasohibin and SVBP, combined with mutagenesis, reveals the residues responsible for substrate recognition and cleavage.
A CDK multisite phosphorylation code ensures that CDK can signal via hundreds of distinct targets to provide a temporally ordered phosphorylation pattern required for proper execution of the cell cycle.
The low-complexity domain of the RNA-binding protein FUS forms dynamic, multivalent interactions via multiple residue types and remains disordered in the densely packed liquid phase.
Crystal structures of the human HMCES SRAP domain in complex with DNA substrates demonstrate how the SRAP domain interacts with a variety of single-strand- and double-strand-containing DNA structures found at DNA-damage sites.
Crystal structures of human vasohibin 1 and 2 in complex with small vasohibin-binding protein (SVBP) in the absence and presence of different inhibitors and a C-terminal α-tubulin peptide define the structural basis of tubulin detyrosination.
A solid-state NMR structure of an amyloid fibril formed by synthetic human glucagon reveals two distinct β-strand conformations that alternate in an antiparallel fashion along the fibril axis.
Structures of human equilibrative nucleoside transporter 1 in complex with either dilazep or NBMPR reveal distinct inhibitory mechanisms of these drugs, providing insight for rational design of improved therapeutics modulating nucleoside transport.
Cryo-EM structures of fibrils formed by two segments from TDP-43 that are essential for aggregation of the full-length protein reveal fibril polymorphism and suggest mechanisms for pathogenesis.