533 results found
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Structure of Vps4 with circular peptides and implications for translocation of two polypeptide chains by AAA+ ATPases

    Han Han et al.
    Structural and biochemical studies indicate that AAA+ ATPase employ a general mechanism to translocate a variety of substrates, including extended polypeptides, hairpins, crosslinked chains, and chains conjugated to other molecules.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    The AAA ATPase Vps4 binds ESCRT-III substrates through a repeating array of dipeptide-binding pockets

    Han Han et al.
    A 3.2 Å resolution structure of Vps4 provides a detailed model for protein substrate binding and translocation by AAA ATPases.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Structural basis of protein translocation by the Vps4-Vta1 AAA ATPase

    Nicole Monroe et al.
    A cryo-electron microscopy structure of a substrate-bound Vps4-Vta1 AAA ATPase reveals an asymmetric hexameric ring and suggests how nucleotide-induced changes in subunit interfaces translocate polypeptides into the central pore.
    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. Structural Biology and Molecular Biophysics
    2. Cell Biology

    Structures of TorsinA and its disease-mutant complexed with an activator reveal the molecular basis for primary dystonia

    F Esra Demircioglu et al.
    High resolution structures of the essential human AAA+ ATPase TorsinA and its disease mutant in complex with an activator reveal details of the interaction that will guide drug design and further functional characterization.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    How lamina-associated polypeptide 1 (LAP1) activates Torsin

    Brian A Sosa et al.
    LAP1 adopts an AAA+ like fold that, while unable to bind nucleotide, can enhance ATPase activity in the neighboring TorsinA protomer in an unusual heterohexameric ring, via an arginine finger.
    1. Structural Biology and Molecular Biophysics
    2. Chromosomes and Gene Expression

    Structure of the active form of human origin recognition complex and its ATPase motor module

    Ante Tocilj et al.
    The human Origin Replication Complex is shaped as a shallow corkscrew in a classic AAA+ organization reminiscent of clamp loader complexes with highly controlled ATPase activity as exemplified by Meier-Gorlin syndrome mutations.
    1. Cell Biology

    The AAA protein Msp1 mediates clearance of excess tail-anchored proteins from the peroxisomal membrane

    Nicholas R Weir et al.
    Msp1, a membrane-integral AAA ATPase at mitochondria and peroxisomes, selectively recognizes uncomplexed substrate molecules in vivo while avoiding substrates stabilized by binding partners.
    1. Cell Biology

    Cooperation of mitochondrial and ER factors in quality control of tail-anchored proteins

    Verena Dederer et al.
    The endoplasmic reticulum E3 ubiquitin ligase Doa10 and the mitochondrial AAA-ATPase Msp1 govern targeting fidelity of outer mitochondrial tail-anchored proteins by controlling cytoplasmic concentration and extracting mistargeted and orphan species.

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