809 results found
    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. 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

    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

    Specific lid-base contacts in the 26s proteasome control the conformational switching required for substrate degradation

    Eric R Greene et al.
    The 26S proteasome lid subcomplex acts as an external scaffold whose interactions with the ATPase motor stabilize the substrate-engagement-competent state, and control conformational changes upon engagement for subsequent degradation steps.
    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

    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.
    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. Biochemistry and Chemical Biology

    Cdc48-like protein of actinobacteria (Cpa) is a novel proteasome interactor in mycobacteria and related organisms

    Michal Ziemski et al.
    Cdc48-like protein of actinobacteria (Cpa) is a AAA+ proteasomal interactor involved in adaptation of mycobacteria to carbon limitation and potentially influencing ribosomal composition of the cell.
    1. Biochemistry and Chemical Biology

    Skd3 (human ClpB) is a potent mitochondrial protein disaggregase that is inactivated by 3-methylglutaconic aciduria-linked mutations

    Ryan R Cupo, James Shorter
    Skd3 (human ClpB) is a potent ATP-dependent mitochondrial protein disaggregase that is activated by the rhomboid protease, PARL, and inactivated by MGCA7-linked mutations.
    1. Biochemistry and Chemical Biology

    The GTPase Nog1 co-ordinates the assembly, maturation and quality control of distant ribosomal functional centers

    Purnima Klingauf-Nerurkar et al.
    The GTPase Nog1 orchestrates stalk assembly, peptidyl transferase centre maturation and polypeptide exit tunnel quality control.

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