3KTH: Structure Of Clpp From Bacillus Subtilis In Orthorombic Crystal Form

Citation:
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.
PDB ID: 3KTHDownload
MMDB ID: 80964
PDB Deposition Date: 2009/11/25
Updated in MMDB: 2010/11
Experimental Method:
x-ray diffraction
Resolution: 3  Å
Source Organism:
Similar Structures:
Biological Unit for 3KTH: heptameric; determined by author and by software (PISA)
Molecular Components in 3KTH
Label Count Molecule
Proteins (7 molecules)
7
Atp-dependent CLP Protease Proteolytic Subunit(Gene symbol: clpP)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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