3tt6 | pdb_00003tt6

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Template:STRUCTURE 3tt6

Structure of ClpP from Bacillus subtilis in compressed state

Template:ABSTRACT PUBMED 22080375

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.[1]

About this Structure

3tt6 is a 7 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

  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
  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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