Full-length ClpX AAA protein in a complex with ClpP peptidase
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ABSTRACT:
SUBMITTER: Alireza Ghanbarpour
PROVIDER: EMPIAR-11706 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
A closed translocation channel in the substrate-free AAA+ ClpXP protease diminishes rogue degradation.
Ghanbarpour Alireza A Cohen Steven E SE Fei Xue X Kinman Laurel F LF Bell Tristan A TA Zhang Jia Jia JJ Baker Tania A TA Davis Joseph H JH Sauer Robert T RT
Nature communications 20231110 1
AAA+ proteases degrade intracellular proteins in a highly specific manner. E. coli ClpXP, for example, relies on a C-terminal ssrA tag or other terminal degron sequences to recognize proteins, which are then unfolded by ClpX and subsequently translocated through its axial channel and into the degradation chamber of ClpP for proteolysis. Prior cryo-EM structures reveal that the ssrA tag initially binds to a ClpX conformation in which the axial channel is closed by a pore-2 loop. Here, we show tha ...[more]
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