Article
Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations.
Structure (London, England : 1993) - 14 Jul 2010
Kimber Matthew S, Yu Angela Yeou Hsiung, Borg Mikael, Leung Elisa, Chan Hue Sun, Houry Walid A
Abstract excerpt
The highly conserved ClpP protease consists of two heptameric rings that interact by the interdigitation of an alpha-helix beta strand handle domain motif to form a tetradecameric cylinder. We previously proposed that protease dynamics results in the temporary unstructuring of interacting pairs of handle domains, opening transient equatorial side pores that allow for peptide egress. Here, we report the structure...
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