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Cryo-EM structures of human ATP-citrate lyase alone or bound to substrates or products and supportive biochemical and biophysical data reveal the catalytic mechanism of this enzyme, which is the major source of cytosolic acetyl-CoA.
Ancestral reconstruction leads to characterization and crystallization of three ancient mammalian flavin-containing monooxygenases, offering insights into their mechanisms of membrane binding, catalytic activity and substrate selection.
Cryo-EM structure of human transporter ABCB4 that extrudes phosphatidylcholine into the bile canaliculi suggests an ‘alternating access’ mechanism of lipid extrusion, distinct from the ‘credit card swipe’ model of other lipid transporters.
Cryo-EM and functional analyses of human CTP synthase 2 reveal that this enzyme forms polymeric filaments that can switch between active and inactive forms, in response to substrate and product levels, resulting in highly cooperative regulation.
The crystal structure of a posttermination 70S ribosome complex with EF-G, RRF and two tRNAs bound reveals the active roles played by those factors in ribosome splitting and recycling.
Structural, biochemical and cellular analyses show that bacterial antigens can mimic gliadin epitopes involved in celiac disease being presented by HLA-DQ2.5 and recognized by T cells derived from patients.
The cryo-EM structure of the PWWP reader domain of the transcriptional coactivator LEDGF in complex with an H3K36-methylated nucleosome reveals multivalent binding of the reader domain to the methylated histone tail and to both gyres of nucleosomal DNA.
Cryo-EM resolution of HIV-1 Env trimer bound to CD4 and a tyrosine-sulfated, coreceptor-mimicking antibody reveals two configurations of gp120–gp41 protomers that create asymmetric Env trimer conformations on the path to membrane fusion.
Oligomers of human αA-crystallin are characterized structurally via a hybrid approach, combining cryo-EM, cross-linking/mass spectrometry, NMR and modeling, providing insight into their dynamic behavior and heterogeneity and revealing that oxidized oligomers can also act as chaperones.
The cocrystal structure of the Nocardia farcinicaileS T-box in complex with its cognate tRNA illustrates how mRNA junctions can create specific binding sites for interacting RNAs.
The structure of human SMG1–SMG8–SMG9, a PI(3)K-related protein kinase complex central to mRNA surveillance, uncovers an InsP6-binding site in the SMG1 kinase that is conserved in mTOR and important for kinase activity.
Cryo-EM structure of the C-terminal domain of human APOBEC3F in complex with HIV-1 Vif and CFBβ, along with functional analyses, reveals how Vif targets a host restriction protein.
Cryo-EM structures of MERS-CoV S glycoprotein trimer in complex with different sialosides reveal how the virus engages with sialylated receptors, providing insight into receptor specificity and selectivity.
Biochemical and structural analysis demonstrate that simultaneous detection of poly-lysine in the exit tunnel and poly(A) in the decoding center allows ribosomes to detect aberrant mRNAs, stall elongation and trigger downstream quality control pathways.
Cocrystal and cryo-EM structures of Geobacillus kaustophilus glyQ and Bacillus subtilis glyQS T-box-tRNA complexes establish a universal mechanism of amino acid sensing on tRNAs and gene regulation by T-box riboswitches.
High-resolution cryo-EM structures of the core TOM complex from Saccharomyces cerevisiae, as dimeric and tetrameric assemblies, provide new insights into the mechanism of protein translocation into mitochondria.
The cryo-EM structure of a megacomplex between chimeric GPCR, G protein and β-arrestin in their canonical active conformations provides insight into the basis of sustained G protein signaling upon megacomplex internalization.
The crystal structure of the full-length ileS T-box–tRNA complex from Mycobacterium tuberculosis provides a complete high-resolution explanation of tRNA decoding and aminoacylation sensing by this riboregulator.
CRISPR–Cas9-based method to introduce site-specific S-GlcNAcylation enables dissection of the roles of protein O-GlcNAcylation. S-GlcNAc, a hydrolytically stable structural mimic of O-GlcNAc, is recognized by a range of O-GlcNAc-binding proteins.
Cryo-EM analyses of α-synuclein fibrils formed with hereditary Parkinson’s disease mutant H50Q reveal features that help explain the mutant’s properties in vitro and in cells.