ATP-dependent Clp protease adaptor protein
FunctionATP-dependent Clp protease adaptor protein (ClpS) influences the protein degradation by binding to the chaperone-protease ClpAP toward degradation of aggregated proteins[1]. Degradation susceptibility is related to N-terminal residues. It is formulated by the N-end rule[2]. In bacteria the residues are Tyr, Phe, Trp and Leu. ClpS binds these residues and delivers the protein to degradation by ClpAP[3]. Structural highlights[4].
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3D Structures of ATP-dependent Clp protease adaptor protein3D Structures of ATP-dependent Clp protease adaptor protein
Updated on 22-November-2017
3o2o, 3o1f – EcClpS – Escherichia coli
1r6o, 1r6q – EcClpS + ClpA
3o2b, 3o2h, 2wa9, 2w9r, 2wa8 – EcClpS + peptide
3gq0 – CvClpS – Caulobacter vibrioides
3g19, 3gq1, 3gw1, 3dnj – CvClpS + peptide
3g1b, 3g3p – CvClpS (mutant) + peptide
4yjm – AtClpS 2 – Agrobacterium tumefaciens
4yjx, 4yka – AtClpS 2 + amino acid
ReferencesReferences
- ↑ Dougan DA, Reid BG, Horwich AL, Bukau B. ClpS, a substrate modulator of the ClpAP machine. Mol Cell. 2002 Mar;9(3):673-83. PMID:11931773
- ↑ Varshavsky A. Discovery of cellular regulation by protein degradation. J Biol Chem. 2008 Dec 12;283(50):34469-89. doi: 10.1074/jbc.X800009200. Epub 2008, Aug 15. PMID:18708349 doi:http://dx.doi.org/10.1074/jbc.X800009200
- ↑ Schuenemann VJ, Kralik SM, Albrecht R, Spall SK, Truscott KN, Dougan DA, Zeth K. Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS. EMBO Rep. 2009 May;10(5):508-14. Epub 2009 Apr 17. PMID:19373253 doi:10.1038/embor.2009.62
- ↑ Dougan DA, Reid BG, Horwich AL, Bukau B. ClpS, a substrate modulator of the ClpAP machine. Mol Cell. 2002 Mar;9(3):673-83. PMID:11931773