Browse our latest Structural Biology and Molecular Biophysics articles

Page 123 of 178
    1. Structural Biology and Molecular Biophysics

    Asymmetry of movements in CFTR's two ATP sites during pore opening serves their distinct functions

    Ben Sorum, Beáta Töröcsik, László Csanády
    In the CFTR chloride channel, ATP bound in the catalytic site promotes pore opening, whereas ATP bound in the non-catalytic site supports unidirectional conformational cycling by preventing pore closure without ATP hydrolysis in the catalytic site.
    1. Structural Biology and Molecular Biophysics
    2. Neuroscience

    The P2X7 receptor forms a dye-permeable pore independent of its intracellular domain but dependent on membrane lipid composition

    Akira Karasawa, Kevin Michalski ... Toshimitsu Kawate
    Functional reconstitution of a mammalian P2X7 receptor uncovers an intrinsic and lipid-dependent dye-permeable membrane pore.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Site-specific monoubiquitination downregulates Rab5 by disrupting effector binding and guanine nucleotide conversion

    Donghyuk Shin, Wooju Na ... Sangho Lee
    With monoubiquitination sites of Rab5 identified and structural and biochemical studies using chemically synthesized ubiquitinated Rab5, Rab5 monoubiquitination is found to downregulate the function of Rab5 in a site-dependent manner.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Dynamics and consequences of spliceosome E complex formation

    Joshua Donald Larson, Aaron A Hoskins
    Single molecule fluorescence analysis of spliceosome E complex formation reveals how tuning of U1 binding to the 5' SS facilitates efficient capture of the snRNP by pre-mRNAs.
    1. Structural Biology and Molecular Biophysics

    Rac1 GTPase activates the WAVE regulatory complex through two distinct binding sites

    Baoyu Chen, Hui-Ting Chou ... Michael K Rosen
    The cryo-electron microscopy structure of an assembly of the WAVE Regulatory Complex and its activator, the Rac GTPase, plus complementary biochemistry and biophysics, reveal a novel activation mechanism involving two distinct Rac binding sites.
    1. Structural Biology and Molecular Biophysics

    Acidic C-terminal domains autoregulate the RNA chaperone Hfq

    Andrew Santiago-Frangos, Jeliazko R Jeliazkov ... Sarah A Woodson
    Modeling and biophysics show that the unstructured acidic tail of the Sm protein Hfq mimics nucleic acid to auto inhibit its chaperone activity, preventing Hfq from being sequestered by inauthentic substrates and providing insight into the evolution of Hfq's chaperone function among bacterial genera.
    1. Structural Biology and Molecular Biophysics

    Autoinhibition of ankyrin-B/G membrane target bindings by intrinsically disordered segments from the tail regions

    Keyu Chen, Jianchao Li ... Mingjie Zhang
    The 24 ANK repeats of each ankyrin are inhibited by combinatorial bindings of multiple disordered segments from their tail regions, suggesting a mechanism for differential regulations of membrane target bindings by ankyrins.
    1. Structural Biology and Molecular Biophysics
    2. Microbiology and Infectious Disease

    Structural dynamics of RbmA governs plasticity of Vibrio cholerae biofilms

    Jiunn CN Fong, Andrew Rogers ... Fitnat H Yildiz
    Biofilm matrix protein RbmA controls biofilm architecture through binary structural switching and exopolysaccharide binding.
    1. Structural Biology and Molecular Biophysics
    2. Microbiology and Infectious Disease

    Biofilms: Flipping the switch

    Xavier Pierrat, Alexandre Persat
    A structural switch controls the architecture of Vibrio cholerae biofilms by mediating the interactions between two matrix components.
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    1. Structural Biology and Molecular Biophysics

    The divergent mitotic kinesin MKLP2 exhibits atypical structure and mechanochemistry

    Joseph Atherton, I-Mei Yu ... Carolyn A Moores
    MKLP2 is a divergent molecular motor that has structurally evolved to bind its microtubule track and use the energy of ATP in distinct ways, tuned according to its function in cell division.