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Showing 1–10 of 10 results
Advanced filters: Author: Borries Demeler Clear advanced filters

  • Cannulae are heat-resistant protein nanotubes found on the surface of thermophilic archaea. Here, the authors report the structures of cannulae at the atomic level with insight into their high stability and mechanism of assembly, which has potential impact for biomaterials design.

    • Mike Sleutel
    • Ravi R. Sonani
    • Vincent P. Conticello
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-18

  • ComEA is a DNA-binding protein required for DNA uptake during bacterial transformation. Here, Ahmed et al. determine X-ray crystal structures of ComEA from Gram-positive bacteria, identifying a domain that is absent in Gram-negative bacteria and drives ComEA oligomerization, which is required for transformation.

    • Ishtiyaq Ahmed
    • Jeanette Hahn
    • Matthew B. Neiditch
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-14

  • As biochemistry ventures out from its reductionist roots, concentration effects and high surface-to-volume ratios will challenge our current understanding of biological systems, with colloidal and surface chemistry leading to new insights and approaches. How must our thinking change, what new tools will we need and how will these new tools be developed?

    • Tom Laue
    • Borries Demeler
    Comments & Opinion
    Nature Chemical Biology
    Volume: 7, P: 331-334

  • The GntR superfamily is one of the largest families of transcription factors in prokaryotes. Here the authors combine biophysical analysis and structural biology to dissect the mechanism by which NanR — a GntR-family regulator — binds to its promoter to repress the transcription of genes necessary for sialic acid metabolism.

    • Christopher R. Horne
    • Hariprasad Venugopal
    • Renwick C. J. Dobson
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-16

  • SAMHD1 catalyses the dephosphorylation of deoxynucleotide triphosphates (dNTPs) and has antiretroviral activity. Here, the authors present the crystal structures of SAMHD1-oligonucleotide complexes, which reveal that the allosteric binding sites of SAMHD1 are plastic and can fit oligonucleotides in place of the two allosteric activators GTP and dNTP, and they also show that SAMHD1 recognises GpsN phosphorothioation modifications in nucleic acids, which is of interest in drug design.

    • Corey H. Yu
    • Akash Bhattacharya
    • Dmitri N. Ivanov
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-14

  • BMI1, a core element of the polycomb repressive complex 1, is suggested to have oncogenic activity in a variety of cancers. Here, the authors report the structure of BMI1 bound to the protein PHC2, identify BMI1 homo-oligomerization interfaces, and analyse the role of BMI1 protein-protein interactions in PRC1 function.

    • Felicia Gray
    • Hyo Je Cho
    • Tomasz Cierpicki
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-12

  • The first crystal structure and in vitro biochemical characterization of an enoylreductase domain from a multimodular polyketide synthase indicates substantial architectural deviations from the mammalian fatty acid synthase and identifies an active site residue that controls catalytic activity.

    • Jianting Zheng
    • Darren C Gay
    • Adrian T Keatinge-Clay
    Research
    Nature Chemical Biology
    Volume: 8, P: 615-621

  • Heterochromatin is a ‘repressed’ chromatin state involved in the generation of centromeres, the protection of telomeres and the maintenance of genome integrity. Here Swygert et al.show that Sir3 - a key factor in the formation of heterochromatin - promotes a chromatin structure distinct from the canonical 30 nm fibre.

    • Sarah G. Swygert
    • Benjamin J. Manning
    • Craig L. Peterson
    Research
    Nature Communications
    Volume: 5, P: 1-12