57 results found
    1. Structural Biology and Molecular Biophysics

    Structural basis of ClpXP recognition and unfolding of ssrA-tagged substrates

    Xue Fei et al.
    Cryo-EM structures of the AAA+ ClpXP protease bound to an ssrA degron reveal the mechanism of substrate recognition and show how the machine transitions from recognition to translocation and unfolding.
    1. Structural Biology and Molecular Biophysics

    Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate

    Xue Fei et al.
    Cryo-EM structures of the ClpXP protease reveal how protein substrates are bound, show how spiral ClpX hexamers bind symmetry-mismatched heptameric ClpP rings, and suggest mechanisms for processive substrate translocation.
    1. Structural Biology and Molecular Biophysics

    A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery

    Zev A Ripstein et al.
    Understanding of bacterial protein degradation is illuminated by cryo-EM structures of the substrate-bound ClpXP complex from Neisseria meningitidis at 2.3 to 3.3 Å resolution.
    1. Biochemistry and Chemical Biology

    Mitochondrial ClpX activates an essential biosynthetic enzyme through partial unfolding

    Julia R Kardon et al.
    The mitochondrial protein unfoldase ClpX activates the first enzyme in heme biosynthesis, ALAS, by targeted unfolding that gates access of cofactor to the ALAS active site.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    ClpAP proteolysis does not require rotation of the ClpA unfoldase relative to ClpP

    Sora Kim et al.
    Crosslinking the AAA+ protease interface does not abolish protein degradation by ClpAP, establishing that rotation of the AAA+ unfoldase with respect to its partner peptidase is not essential for activity.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Interactions between a subset of substrate side chains and AAA+ motor pore loops determine grip during protein unfolding

    Tristan A Bell et al.
    The AAA+ protein unfolding motor ClpX grips substrates with the uppermost part of its substrate-binding pore, and requires interactions with hydrophobic amino acid side chains to operate with optimal efficiency.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    TRIP13 is a protein-remodeling AAA+ ATPase that catalyzes MAD2 conformation switching

    Qiaozhen Ye et al.
    TRIP13 inactivates the spindle assembly checkpoint by converting MAD2 from its active ‘closed’ state to its inactive ‘open’ state.
    1. Microbiology and Infectious Disease

    PrkA controls peptidoglycan biosynthesis through the essential phosphorylation of ReoM

    Sabrina Wamp et al.
    Analysis of suppressor mutants led to the identification of a novel signalling pathway that regulates peptidoglycan biosynthesis in Gram-positive bacteria.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation

    Marta Carroni et al.
    Overcoming image-processing problems in the analysis of the ClpB chaperone provides a new structural model and regulatory mechanism, based on clear density for the coiled-coil domain and supported by various biochemical data.
    1. Biochemistry and Chemical Biology

    Regulatory coiled-coil domains promote head-to-head assemblies of AAA+ chaperones essential for tunable activity control

    Marta Carroni et al.
    Head-to-head interactions of regulatory coiled-coil domains control activity of the central bacterial AAA+ protein ClpC by promoting formation of a reversible resting state.

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