Proteopedia

ATP-dependent Clp protease adaptor protein


Function

ATP-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].

3D Structures of ATP-dependent Clp protease adaptor protein

ATP-dependent Clp protease adaptor protein 3D structures


E. coli ClpS (deep sky blue) complex with peptide (green) (PDB code 3o2h)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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

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