|Nature Structural aamp; Molecular Biology - Issue - nature.com science feeds|
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.
The crystal structure of the Atg101–Atg13 complex elucidates the function of Atg101 and sheds light on the molecular mechanisms of autophagy initiation in higher eukaryotes.
The crystal structure of human stearoyl-CoA desaturase-1 in complex with its natural substrate provides a close-up view of a key enzymatic step in the synthesis of unsaturated fatty acids.
|Nature Structural aamp; Molecular Biology - AOP - nature.com science feeds|
Plasmepsin V is an aspartyl protease essential for export of effector proteins to Plasmodium-infected erythrocytes. A new inhibitor blocks plasmepsin V and inhibits parasite growth; it has also allowed solving the structure of P. vivax plasmepsin V.
Structural studies of human polysialyltransferase ST8SialII in apo form and in complex with donor sugar and sulfated glycan acceptor shed light on the substrate binding and specificity as well as the catalytic activity of this class of polysialyltransferases.
NMR relaxation dispersion measurements reveal the conformational dynamics of the mitochondrial ADP/ATP carrier and show that the ADP substrate facilitates interconversion between the predominant cytosol-facing state and a sparsely populated excited state.
Chromatin reassembly after replication requires recycling of old and deposition of new histones. Structural insights into how MCM2, part of the replicative helicase, interacts with H3–H4 suggest a function in histone recycling at replication forks.
Chemical genetics, proteomics and biochemistry are used to probe the functions of SR protein kinases. An identified target of Dsk1 is spliceosomal protein Bpb1 (SF1), whose phosphorylation increased its binding to introns with nonconsensus splice sites.
Structural analyses capture RING E3 ligase RNF4 bound to Ube2V2–Ubc13 E2 complex charged with ubiquitin and, along with functional assays, reveal the basis for synthesis of K63-linked chains.
Extensive glycan microarray and structural analyses reveal that human intelectin-1 interacts selectively with microbial glycan epitopes through recognition of a terminal 1,2-diol group, an interaction that would be blocked in human glycans such asα-Neu5Ac.
Flexible filamentous plant viruses, which cause substantial crop damage worldwide, have eluded structural characterization so far. The cryo-EM structure of BaMV now reveals the virus architecture and the structural basis of its flexibility.