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Molecular Architecture and Functional Analysis of NetB, a Pore-forming Toxin from Clostridium perfringens*
The crystal structure of the pore form of NetB is presented, showing that NetB does not bind phosphocholine efficiently but instead interacts directly with cholesterol leading to enhanced oligomerization and pore formation and providing potential new tools to the field of bionanotechnology. Expand
Structural Changes Enable Start Codon Recognition by the Eukaryotic Translation Initiation Complex
A cryoEM reconstruction of a yeast preinitiation complex at 4.0 Å resolution with initiator tRNA in the PIN state reveals stabilization of the codon-anticodon duplex by the N-terminal tail of eIF1A, changes in the structure of e IF1 likely instrumental in its subsequent release, and changed in the conformation of eif2. Expand
Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase
The three-dimensional structure of the SecA protein of Mycobacterium tuberculosis is reported, which predicts that SecA can interact with the SecYEG pore and function as a molecular ratchet that uses ATP hydrolysis for physical movement of the preprotein. Expand
Burkholderia cenocepacia phage BcepMu and a family of Mu-like phages encoding potential pathogenesis factors.
We have isolated BcepMu, a Mu-like bacteriophage whose host range includes human pathogenic Burkholderia cenocepacia (formally B. cepacia genomovar III) isolates, and determined its complete 36748 bpExpand
Molecular basis of toxicity of Clostridium perfringens epsilon toxin
The exquisite specificity of the toxin for specific cell types suggests that it binds to a receptor found only on these cells, and the crystal structure of ε‐toxin reveals similarity to aerolysin from Aeromonas’hydrophila, parasporin‐2 from Bacillus’thuringiensis and a lectin from Laetiporus’sulphureus. Expand
Holin triggering in real time
It is suggested that phage lysis occurs when the holin reaches a critical concentration and nucleates to form rafts, analogous to the initiation of purple membrane formation after the induction of bacteriorhodopsin in halobacteria. Expand
The architecture of the spliceosomal U4/U6.U5 tri-snRNP
Cryo-electron microscopy single-particle reconstruction of Saccharomyces cerevisiae tri-snRNP is used to reveal the essentially complete organization of its RNA and protein components, providing crucial insights into the activation process and the active site of the spliceosome. Expand
The terminase subunits pUL56 and pUL89 of human cytomegalovirus are DNA-metabolizing proteins with toroidal structure.
A first characterization of the terminase subunits pUL56 and pUL89 of human cytomegalovirus (HCMV) is reported, providing the first insights into theterminase-dependent viral DNA-packaging mechanism of HCMV. Expand
Structure of a bacterial type IV secretion core complex at subnanometre resolution
The I‐layer structure is determined using high‐resolution cryo‐electron microscopy and molecular modelling combined with biochemical approaches, which provides new structural insights on the CC, from which the essential features of T4S system mechanisms can be derived. Expand
Structural characterization of ribosome recruitment and translocation by type IV IRES
Using electron cryomicroscopy, the structure explains how diphthamide, a eukaryotic and archaeal specific post-translational modification of a histidine residue of eEF2, is involved in translocation. Expand