Journal article
Acyldepsipeptide Antibiotics Induce the Formation of a Structured Axial Channel in ClpP: A Model for the ClpX/ClpA-Bound State of ClpP
Abstract
In ClpXP and ClpAP complexes, ClpA and ClpX use the energy of ATP hydrolysis to unfold proteins and translocate them into the self-compartmentalized ClpP protease. ClpP requires the ATPases to degrade folded or unfolded substrates, but binding of acyldepsipeptide antibiotics (ADEPs) to ClpP bypasses this requirement with unfolded proteins. We present the crystal structure of Escherichia coli ClpP bound to ADEP1 and report the structural changes …
Authors
Li DHS; Chung YS; Gloyd M; Joseph E; Ghirlando R; Wright GD; Cheng Y-Q; Maurizi MR; Guarné A; Ortega J
Journal
Cell Chemical Biology, Vol. 17, No. 9, pp. 959–969
Publisher
Elsevier
Publication Date
September 2010
DOI
10.1016/j.chembiol.2010.07.008
ISSN
2451-9456