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    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Disease-related mutations in PI3Kγ disrupt regulatory C-terminal dynamics and reveal a path to selective inhibitors

    Manoj K Rathinaswamy et al.
    The c-terminus of PI3K plays a key role in regulating kinase activity, with c-terminal disease-linked mutations leading to either activation or inhibition, which reveal a path to specific inhibitors.
    1. Structural Biology and Molecular Biophysics

    Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins

    Joseph Atherton et al.
    Cryo-electron microscopy reconstructions of two microtubule-bound transport kinesins at 7 Å resolution reveal how microtubule track binding stimulates ADP release, primes the active site for ATP binding and enables force generation.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Structural insights into the molecular mechanism of the m6A writer complex

    Paweł Śledź, Martin Jinek
    The structure of the catalytic core of the N6-methyladenosine RNA methyltransferase complex METTL3-METTL14 reveals that METTL3 is the catalytic subunit, while METTL14 plays non-catalytic roles in substrate recognition and in maintaining complex integrity.
    1. Cell Biology

    The RhoGAP activity of CYK-4/MgcRacGAP functions non-canonically by promoting RhoA activation during cytokinesis

    Donglei Zhang, Michael Glotzer
    Activation of the key regulator of cytokinesis, RhoA, involves an unexpected contribution by a RhoGAP domain.
    1. Structural Biology and Molecular Biophysics
    2. Computational and Systems Biology

    A dynamic mechanism for allosteric activation of Aurora kinase A by activation loop phosphorylation

    Emily F Ruff et al.
    Phosphorylation of Aurora A does not trigger a population shift to the active state as previously thought, but instead switches the kinase on by tuning the structure and dynamics of a dynamically sampled subpopulation.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Structural basis for interdomain communication in SHIP2 providing high phosphatase activity

    Johanne Le Coq et al.
    The SHIP2 inositol phosphatase is an important upstream regulator of the Akt signaling pathway, which requires a catalytic core formed by the phosphatase domain tightly packed to a C2 domain for its function.
    1. Biochemistry and Chemical Biology
    2. Microbiology and Infectious Disease

    A widespread family of serine/threonine protein phosphatases shares a common regulatory switch with proteasomal proteases

    Niels Bradshaw et al.
    Structures of active and inactive conformations of a PP2C family phosphatase reveal a conserved switch that controls enzymatic activity and point to an unexpected relationship between phosphatases and proteasomal proteases.
    1. Structural Biology and Molecular Biophysics

    Structural insights into SETD3-mediated histidine methylation on β-actin

    Qiong Guo et al.
    Structural research, supplemented by biochemical experiments and enzymatic assays, unravels the sequence-dependent molecular mechanism by which SETD3 recognizes β-actin and methylates His73 of β-actin.
    1. Structural Biology and Molecular Biophysics
    2. Chromosomes and Gene Expression

    Structural snapshots of Xer recombination reveal activation by synaptic complex remodeling and DNA bending

    Aleksandra Bebel et al.
    DNA-bound crystal structures of an essential Xer site-specific recombinase from the bacterium Helicobacter pylori reveal how large conformational changes initiate the untangling of chromosomes upon cell division.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Molecular basis for catabolism of the abundant metabolite trans-4-hydroxy-L-proline by a microbial glycyl radical enzyme

    Lindsey RF Backman et al.
    The common post-translational modification trans-4-hydroxy-L-proline is reversed by gut microbes with the help of hydroxyproline dehydratase (HypD), an enzyme that performs a radical chemical mechanism.