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Showing 1–15 of 15 results

    • Michelle Montoya
    Research Highlights
    Nature Structural & Molecular Biology
    Volume: 20, P: 922

  • Biomolecular condensates compartmentalize and concentrate cellular components without the delimitation of a lipid membrane. The protein VASP is now shown to condense, resulting in the reorganization of actin, a key component of the cell cytoskeleton.

    • Julie Plastino
    News & Views
    Nature Physics
    Volume: 19, P: 477-478

  • Recent studies offer new insight on the mechanisms of IP6-mediated HIV-1 capsid assembly. The immature Gag lattice enables enrichment of IP6 into virions, aiding capsid maturation. Structures of capsid protein (CA) assemblies reveal motifs serving as switches modulating the conformations of CA pentamers/hexamers and affect co-factor accessibility.

    • Chunxiang Wu
    • Yong Xiong
    News & Views
    Nature Structural & Molecular Biology
    Volume: 30, P: 239-241

  • Light-activated protein actuators composed of bioengineered motors and molecular scaffolds achieve millimetre-scale mechanical work, which holds promise for microrobotics applications.

    • Henry Hess
    News & Views
    Nature Materials
    Volume: 20, P: 1040-1041

  • Cryo-EM analysis reveals the mechanism by which chromatin is compacted at the centromere by the H3 histone variant CENP-N. Intriguingly, despite the structural differences between CENP-N and linker H1 histones, both appear to similarly compact higher-order nucleosome structures.

    • Katrina V. Good
    • Juan Ausió
    News & Views
    Nature Structural & Molecular Biology
    Volume: 29, P: 288-290

  • A new cryo-EM structure of the bacterial flagellar hook, which connects the motor to the flagellar filament, reveals 11 distinctive conformations of the subunit. The cooperative dynamic switching among these states offers a dramatic extension of two-state models of protein allostery.

    • Edward H. Egelman
    News & Views
    Nature Structural & Molecular Biology
    Volume: 26, P: 848-849

  • Proteins can self-assemble into functional states, or they can end up as aberrant and sometimes toxic aggregates. Metastable intermediate states are often detected in these processes, and their structural characterization provides vital information about the balance between functional and pathological behavior in living systems.

    • Michele Vendruscolo
    • Christopher M Dobson
    News & Views
    Nature Chemical Biology
    Volume: 9, P: 216-217

  • Control of protein self-assembly and disassembly, which is central to metabolism and engineering applications, remains challenging. Here, a perspicacious redesign of interfaces in the multisubunit ferritin protein cage provides single, modifiable subunits that assemble with Cu2+ templating and give insights into the cage assembly code.

    • Elizabeth C Theil
    • Paola Turano
    News & Views
    Nature Chemical Biology
    Volume: 9, P: 143-144

  • All current evidence indicates a central role for α-synuclein (α-SYN) amyloid fibrils in Parkinson's disease and other synucleinopathies, but the precise relationship between amyloid aggregates and the resulting phenotype remains poorly understood, partly because of the lack of reliable three-dimensional structures. In this issue, the structure of a toxic α-SYN fibril is now presented at unprecedented resolution.

    • Wouter Peelaerts
    • Veerle Baekelandt
    News & Views
    Nature Structural & Molecular Biology
    Volume: 23, P: 359-360

  • Iron-sulfur (Fe-S) clusters are among nature's simplest and most versatile agents of electron transfer. Remarkably, their biological assembly involves an obligatory electron transfer event. It is now revealed that parallel but distinct electron transfer pathways are separately required for compartment-specific Fe-S protein maturation.

    • Patricia C Dos Santos
    • Dennis R Dean
    News & Views
    Nature Chemical Biology
    Volume: 6, P: 700-701

  • Self-assembly of the COPII coat proteins Sec13 and Sec31 creates a spherical cage that drives vesicle formation from the endoplasmic reticulum. A multipronged approach now provides a convincing pseudoatomic model of the assembled cage that sharpens our understanding of the architecture, contact sites and flexibility of this remarkable structure.

    • Elizabeth A. Miller
    News & Views
    Nature Structural & Molecular Biology
    Volume: 20, P: 139-140