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Showing 1–23 of 23 results
Advanced filters: Author: Justin Kollman Clear advanced filters
  • Host antibodies can alter the glycan binding of adhesin proteins from infectious bacteria, but the antibodies’ mechanisms of action remain unclear. Here, the authors define four mechanisms of modulation, including ligand mimicry and multiple modes of allosteric interference.

    • Kelli L. Hvorecny
    • Gianluca Interlandi
    • Justin M. Kollman
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-15
  • Engineering the tunability of protein assembly in response to pH changes within a narrow range is challenging. Here the authors report the de novo computational design of pH-responsive protein filaments that exhibit rapid, precise, tunable and reversible assembly and disassembly triggered by small pH changes.

    • Hao Shen
    • Eric M. Lynch
    • David Baker
    ResearchOpen Access
    Nature Nanotechnology
    Volume: 19, P: 1016-1021
  • Actin is critical to the survival of the parasite Toxoplasma gondii. In this study, Hvorecny and Sladewski et al. show that T. gondii actin forms intrinsically dynamic filaments in vitro due to differences in assembly contacts in the D-loop.

    • Kelli L. Hvorecny
    • Thomas E. Sladewski
    • Aoife T. Heaslip
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-16
  • CD163, a macrophage receptor, is essential for clearing hemoglobin during hemolysis to prevent oxidative damage. Here, the authors reveal the cryo-electron microscopy structure of CD163 bound to haptoglobin-hemoglobin, uncovering calcium-dependent interactions critical for its function and oligomerization.

    • Anders Etzerodt
    • Jakob Hauge Mikkelsen
    • Christian Brix Folsted Andersen
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-13
  • Here, the authors report the discovery of prophages in cultured SAR11 and show that lysogenic SAR11 produce virions by prophage induction of up to 2.3% of infected cells under carbon-replete growth conditions and up to 30.6% of infected cells under carbon-deplete conditions.

    • Robert M. Morris
    • Kelsy R. Cain
    • Justin M. Kollman
    Research
    Nature Microbiology
    Volume: 5, P: 1011-1015
  • Here, the authors provide structural insights into the regulation of the gate-keeper glycolytic enzyme phosphofructokinase-1, including the molecular mechanisms of its allosteric regulation and assembly into higher-order filaments.

    • Eric M. Lynch
    • Heather Hansen
    • Bradley A. Webb
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-12
  • Cryo-EM of human PRPS1 shows the nucleotide-synthesizing enzyme assembling into filaments that accommodate active and inhibited conformations. Engineered and disease mutations reveal that filament assembly stabilizes allosteric sites, enhancing catalytic activity.

    • Kelli L. Hvorecny
    • Kenzee Hargett
    • Justin M. Kollman
    Research
    Nature Structural & Molecular Biology
    Volume: 30, P: 391-402
  • A study describes an approach using designed building blocks that are far more regular in geometry than natural proteins to construct modular multicomponent protein assemblies.

    • Timothy F. Huddy
    • Yang Hsia
    • David Baker
    ResearchOpen Access
    Nature
    Volume: 627, P: 898-904
  • The prediction of interatomic potentials by machine learning is a well developed method; however, interatomic potentials account for only the energies and atomic forces and neglect other essential chemical properties. This Review showcases how other properties of interest, such as atomic charges, dipole moments, long-range effects, bond orders and parameters of reduced Hamiltonians, can also be accurately predicted using machine learning models.

    • Nikita Fedik
    • Roman Zubatyuk
    • Sergei Tretiak
    Reviews
    Nature Reviews Chemistry
    Volume: 6, P: 653-672
  • XXXMicrotubules are nucleated in vivo by γ-tubulin complexes and comprise 13 protofilaments. How this precise geometry is controlled remains unclear. These authors report the cryo-electron microscopic structure of the universally conserved, core microtubule nucleating complex, γ-tubulin small complex. The structure provides insight into how this complex establishes thirteen-fold tubulin symmetry.

    • Justin M. Kollman
    • Jessica K. Polka
    • David A. Agard
    Research
    Nature
    Volume: 466, P: 879-882
  • An approach for the design of protein pores is demonstrated by the computational design and subsequent experimental expression of both an ion-selective and a large transmembrane pore.

    • Chunfu Xu
    • Peilong Lu
    • David Baker
    Research
    Nature
    Volume: 585, P: 129-134
  • Previous models of γ-tubulin ring complex (γTuRC) assembly implied that γ-tubulin complex proteins (GCPs) 4–6 serve as a scaffold for arranging multiple γ-tubulin small complexes (γTuSCs) into large γTuRCs. The crystal structure of human GCP4 represents a prototype for all GCPs and can be precisely positioned within γTuSC, providing a new framework for understanding γTuRC formation.

    • Valérie Guillet
    • Martine Knibiehler
    • Lionel Mourey
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 915-919
  • Structural and functional analyses of BRCA1/BARD1 E3 ligase interactions with the H2A C-terminal tail reveal both the basis of its substrate specificity and the consequences of cancer-associated BRCA1/BARD1 mutations.

    • Samuel R. Witus
    • Anika L. Burrell
    • Rachel E. Klevit
    Research
    Nature Structural & Molecular Biology
    Volume: 28, P: 268-277
  • A series of cryo-EM structures of human IMPDH1 variants reveal polymorphic filaments. Blindness-associated mutations in IMPDH1 are characterized and half disrupt feedback inhibition. Together, these findings are a foundation for understanding IMPDH1 in retinal function and disease.

    • Anika L. Burrell
    • Chuankai Nie
    • Justin M. Kollman
    Research
    Nature Structural & Molecular Biology
    Volume: 29, P: 47-58
  • The human enzyme CTP synthase forms polymeric filaments with increased catalytic activity, in contrast to the inactive filaments formed by bacterial CTP synthase. Cryo-EM and crystallographic analyses explain the structural bases for those different behaviors.

    • Eric M Lynch
    • Derrick R Hicks
    • Justin M Kollman
    Research
    Nature Structural & Molecular Biology
    Volume: 24, P: 507-514
  • The γ-tubulin ring complex (γTuRC) nucleates microtubules in the cell. The functional, closed state of yeast γTuRC is now visualized, and its microtubule-nucleating activity is found to be species specific.

    • Justin M Kollman
    • Charles H Greenberg
    • David A Agard
    Research
    Nature Structural & Molecular Biology
    Volume: 22, P: 132-137
  • Microtubule nucleation is regulated by the γ-tubulin small complex (γTuSC) and the γ-tubulin ring complex (γTuRC). Recent structural work, including the crystallographic analysis of γ-tubulin complex protein 4 (GCP4), provides new insights into the mechanism of γTuRC-based microtubule nucleation, confirming the hypothesis that the γTuRC functions as a microtubule template.

    • Justin M. Kollman
    • Andreas Merdes
    • David A. Agard
    Reviews
    Nature Reviews Molecular Cell Biology
    Volume: 12, P: 709-721