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The integral membrane protein stearoyl-CoA desaturase-1 introduces a double bond into stearoyl-CoA during the biosynthesis of unsaturated fatty acids. Crystallographic analysis of human SCD-1 provides atomic details of the interaction with its substrate. Cover design by Erin Dewalt. (pp 581–585)
Two new studies reveal mechanistic insights into how neurons control the assembly of SNARE complexes and the rapid fusion of synaptic vesicles. Structural, biophysical and functional experiments are combined to elucidate the roles of two critical regulators: Munc13 and synaptotagmin.
Asymmetric selection of single-stranded guide RNAs from double-stranded RNA precursors is determined by Ago2, which detects 5′-nucleotide identity and thermodynamic stability of microRNA duplex ends via its MID domain.
The structure of the ligand-free HIV-1–Env trimer allows conformational fixation of Env and generation of an antigen that binds CD4 with high affinity and is recognized by broadly neutralizing antibodies but not poorly neutralizing ones.
New X-ray crystal structure and immunoanalyses of alanyl aminopeptidase N (AnAPN1), a gut antigen of the Anopheles mosquito vector of Plasmodium falciparum, reveal how AnAPN1-specific antibodies block transmission of the malarial parasite.
Biochemical analyses show that in the Escherichia coli type I pilus the plug domain controls activation of usher by masking the substrate-binding site in the C-terminal domains when usher is in resting state.
Crystallographic and functional studies reveal the arch-shaped architecture of the Munc13 MUN domain and show the molecular basis for Munc13's role in synaptic-vesicle priming by mediating syntaxin-1 opening and SNARE-complex assembly.
The NMR-derived structural model of the dynamic interaction between synaptotagmin-1 and the SNARE complex contributes to addressing the longstanding problem of how synaptotagmin-1 triggers neurotransmitter release.
Bacterial energy-coupling factor (ECF) transporters mediate ATP-dependent uptake of essential environmental micronutrients. Biochemical and fluorescence analyses now show that ATP binding promotes release of a substrate-capturing subunit that dynamically reassociates with the transmembrane module during the transport cycle.