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The cryo-EM structure of unliganded mouse NAIP5 reveals the mechanism for NAIP—NLRC4 inflammasome activation in which ligand binding drives a roughly 20° rotation in the WHD–HD2–LRR domains, resulting in the formation of a steric clash to activate NLRC4 and generating new interactions to stabilize the NAIP5–NLRC4 complex.
The flagella of mammalian sperm display non-planar, asymmetric beating, but the molecular basis is unclear. Chen et al. performed in situ cryo-ET of mouse and human sperm and discovered asymmetric distributions of regulatory complexes that could generate asymmetric bending force.
In this paper, the authors discovered and validated aminoacylated lysine ubiquitination and its writer using the genetic code expansion strategy. This non-lysine ubiquitination assembled by UBE2W can mediate rapid protein and proteome degradation.
Kavlashvili et al. use a new in vitro approach to show that uncoupled replication forks can cause fork reversal and nascent strand degradation. Both processes occur without loss of the replisome from DNA and degradation involves multiple steps.
The authors use computational protein design to stabilize the active conformation of cGAS, generating constitutively active cGAS variants that could potentiate prophylactic and therapeutic effects.
In situ cryo-electron tomography reveals the molecular structure of intraflagellar transport (IFT) protein complexes and their assembly into the anterograde IFT trains that build cilia.