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. Author manuscript; available in PMC: 2010 Aug 11.
Published in final edited form as: Biochemistry. 2008 Sep 25;47(42):11031–11040. doi: 10.1021/bi8010169

FIGURE 8. Schematic model showing the gating function of the ClpP N-terminus.

FIGURE 8

A) Degradation by ClpPΔN. After formation of the acyl-enzyme intermediate, the enzyme partitions between an active state that is competent for acyl-enzyme breakdown and an long-lived inactive state (shown in green) in which the acyl-enzyme intermediate is stabilized. Binding of a second substrate to the putative N-terminal binding site accelerates the rate of entry into the active (hydrolysis-competent) state. B) Degradation by ClpAP. ClpA is shown in red, and ClpP is shown in blue. Binding of ClpA causes removal of the ClpP N-terminus from the pore of ClpP, allowing substrates to enter the protease chamber and form the acyl-enzyme intermediate. Re-entry of the N-terminal loops into the ClpP pore causes acyl-enzyme breakdown, and prevents the complex from assuming the inactive conformation.