3kth | pdb_00003kth

Structure of ClpP from Bacillus subtilis in orthorombic crystal form

spinqualitylabelsall models 3kth, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3kth is a 7 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3ktg, 3kti, 3ktj, 3ktk Gene: clpP, yvdN, BSU34540 ("Vibrio subtilis" Ehrenberg 1835) Activity: Endopeptidase Clp, with EC number 3.4.21.92 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CLPP_BACSU] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism.,Lee BG, Park EY, Lee KE, Jeon H, Sung KH, Paulsen H, Rubsamen-Schaeff H, Brotz-Oesterhelt H, Song HK Nat Struct Mol Biol. 2010 Apr;17(4):471-8. Epub 2010 Mar 21. PMID:20305655 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Clp protease 3D structures

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