Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism

Title
Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism
Authors
Byung-Gil LeeEun Young Park이경은전혜성Kwang Hoon SungHolger PaulsenHelga Rubsamen-SchaeHeike Brotz-OesterheHyun Kyu Song
Issue Date
2010-04
Publisher
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Citation
VOL 17, NO 4, 471-478
Abstract
Clp-family proteins are prototypes for studying the mechanism of ATP-dependent proteases because the proteolytic activity of the ClpP core is tightly regulated by activating Clp-ATPases. Nonetheless, the proteolytic activation mechanism has remained elusive because of the lack of a complex structure. Acyldepsipeptides (ADEPs), a recently discovered class of antibiotics, activate and disregulate ClpP. Here we have elucidated the structural changes underlying the ClpP activation process by ADEPs. We present the structures of Bacillus subtilis ClpP alone and in complex with ADEP1 and ADEP2. The structures show the closed-to-open-gate transition of the ClpP N-terminal segments upon activation as well as conformational changes restricted to the upper portion of ClpP. The direction of the conformational movement and the hydrophobic clustering that stabilizes the closed structure are markedly different from those of other ATP-dependent proteases, providing unprecedented insights into the activation of ClpP.
URI
http://pubs.kist.re.kr/handle/201004/40902
ISSN
1545-9985
Appears in Collections:
KIST Publication > Article
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