Featured
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Letter |
Calicivirus VP2 forms a portal-like assembly following receptor engagement
Cryo-electron microscopy structures of feline calicivirus and its cellular receptor show that twelve copies of the minor capsid protein VP2 form a portal-like assembly arranged about a pore in the capsid shell.
- Michaela J. Conley
- , Marion McElwee
- & David Bhella
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Letter |
The BC component of ABC toxins is an RHS-repeat-containing protein encapsulation device
The crystal structure of the complex formed by the B and C toxin complex proteins is reported, revealing how toxin complexes are processed and protected; the proteins assemble to form a large hollow structure that sequesters the cytotoxic portion of the C protein, and a β-propeller domain mediates attachment to the A protein in the native ABC complex.
- Jason N. Busby
- , Santosh Panjikar
- & J. Shaun Lott
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Article |
Accurate assessment of mass, models and resolution by small-angle scattering
Small-angle scattering of X-rays or neutrons is more readily applied to macromolecular complexes than is X-ray crystallography, and is particularly useful for protein complexes with high flexibility; here new quantitative metrics are presented that will allow solution-derived structures to be validated and assessed for mass, resolution and accuracy.
- Robert P. Rambo
- & John A. Tainer
Antiviral signalling by a cyclic nucleotide activated CRISPR protease