3tt7

Structure of ClpP from Bacillus subtilis in complex with DFPStructure of ClpP from Bacillus subtilis in complex with DFP

Template:ABSTRACT PUBMED 22080375

FunctionFunction

[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.^[1]

About this StructureAbout this Structure

3tt7 is a 7 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

ReferenceReference

^{[xtra 1]}

↑ Lee BG, Kim MK, Song HK. Structural insights into the conformational diversity of ClpP from Bacillus subtilis. Mol Cells. 2011 Nov 9. PMID:22080375 doi:10.1007/s10059-011-0197-1

↑ Zellmeier S, Schumann W, Wiegert T. Involvement of Clp protease activity in modulating the Bacillus subtilissigmaw stress response. Mol Microbiol. 2006 Sep;61(6):1569-82. Epub 2006 Aug 8. PMID:16899079 doi:MMI5323

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OCA

[2] Lee BG, Kim MK, Song HK. Structural insights into the conformational diversity of ClpP from Bacillus subtilis. Mol Cells. 2011 Nov 9. PMID:22080375 doi:10.1007/s10059-011-0197-1

[1] Zellmeier S, Schumann W, Wiegert T. Involvement of Clp protease activity in modulating the Bacillus subtilissigmaw stress response. Mol Microbiol. 2006 Sep;61(6):1569-82. Epub 2006 Aug 8. PMID:16899079 doi:MMI5323

[1]

[xtra 1]