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Showing 1–10 of 10 results
Advanced filters: Author: Hari Venugopal Clear advanced filters

  • Many pathogens encode transporters that extract heme directly from host proteins. In this study, the authors demonstrate the utility of de novo-designed proteins in understanding the mechanism behind this process and how it can be inhibited in pathogenic E. coli.

    • Daniel R. Fox
    • Kazem Asadollahi
    • Rhys Grinter
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-15

  • Here the authors show that a gene-inactivating protein complex packs inactive genes into a dynamic and accessible structure. The study challenges the traditional views that restricted accessibility and low dynamics cause gene repression.

    • Michael Uckelmann
    • Vita Levina
    • Chen Davidovich
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 32, P: 520-530

  • Here, Kropp et al. use cryo-electron microscopy and structural modeling to show that the enzyme [MoCu]-CO dehydrogenase interacts with its partner, the membrane-bound quinone-binding protein CoxG, to facilitate electron transfer from atmospheric CO oxidation to the respiratory chain. This interaction is conserved across diverse bacteria and archaea.

    • Ashleigh Kropp
    • David L. Gillett
    • Rhys Grinter
    ResearchOpen Access
    Nature Chemical Biology
    Volume: 21, P: 1058-1068

  • Cryo-electron microscopy structures of the human lysosomal transmembrane protein LYCHOS show that it comprises a transporter-like domain fused to a G-protein-coupled receptor, and that the transporter domain is similar to the plant PIN family.

    • Charles Bayly-Jones
    • Christopher J. Lupton
    • Andrew M. Ellisdon
    ResearchOpen Access
    Nature
    Volume: 634, P: 1238-1244

  • Structural and biochemical studies of the Mycobacterium smegmatis hydrogenase Huc provides insights into how [NiFe] hydrogenases oxidize trace amounts of atmospheric hydrogen and transfer the electrons liberated via quinone transport.

    • Rhys Grinter
    • Ashleigh Kropp
    • Chris Greening
    ResearchOpen Access
    Nature
    Volume: 615, P: 541-547

  • Cryo-EM, X-ray crystallography and crosslinking mass spectrometry are harnessed to solve the structure of the full-length Rho-GEF P-Rex1, uncovering a two-layered mechanism of autoinhibition released upon Gβγ and PI(3,4,5)P3 binding.

    • Yong-Gang Chang
    • Christopher J. Lupton
    • Andrew M. Ellisdon
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 29, P: 767-773

  • Cryo-EM and three-dimensional variability analyses reveal the structure of the autoinhibited 640-kDa NF1 dimer, providing a long-sought-after molecular explanation for the extreme sensitivity of the NF1 gene to loss-of function mutation in disease.

    • Christopher J. Lupton
    • Charles Bayly-Jones
    • Andrew M. Ellisdon
    Research
    Nature Structural & Molecular Biology
    Volume: 28, P: 982-988

  • The glucagon-like peptide-1 receptor (GLP-1R) can be targeted in the treatment of diabetes, obesity and other metabolic disorders. Here, the authors assess the molecular mechanisms of peptide agonists binding to GLP-1R and the responses elucidated by these ligands, including distinct kinetics of G protein activation.

    • Giuseppe Deganutti
    • Yi-Lynn Liang
    • Denise Wootten
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-18