Category:Complex:ClpP serine protease
About
Description (originally from EcoCyc[1]) ClpP serine protease
Comments (originally from EcoCyc[1]) ClpP is a serine protease with a chymotrypsin-like activity that is a part of the ClpAP, ClpAPX and ClpXP protease complexes [2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][9].
References
- ↑ 1.0 1.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ Arribas, J & Castaño, JG (1993) A comparative study of the chymotrypsin-like activity of the rat liver multicatalytic proteinase and the ClpP from Escherichia coli. J. Biol. Chem. 268 21165-71 PubMed
- ↑ Wang, J et al. (1997) The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis. Cell 91 447-56 PubMed
- ↑ Kessel, M et al. (1995) Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome. J. Mol. Biol. 250 587-94 PubMed
- ↑ Shin, DH et al. (1996) Molecular symmetry of the ClpP component of the ATP-dependent Clp protease, an Escherichia coli homolog of 20 S proteasome. J. Mol. Biol. 262 71-6 PubMed
- ↑ Flanagan, JM et al. (1995) Scanning transmission electron microscopy and small-angle scattering provide evidence that native Escherichia coli ClpP is a tetradecamer with an axial pore. Biochemistry 34 10910-7 PubMed
- ↑ Wang, J et al. (1998) Crystal structure determination of Escherichia coli ClpP starting from an EM-derived mask. J. Struct. Biol. 124 151-63 PubMed
- ↑ Thompson, MW et al. (1998) Importance of heptameric ring integrity for activity of Escherichia coli ClpP. Eur. J. Biochem. 258 923-8 PubMed
- ↑ 9.0 9.1 Maurizi, MR et al. (1990) Clp P represents a unique family of serine proteases. J. Biol. Chem. 265 12546-52 PubMed
- ↑ Sprangers, R et al. (2005) Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release. Proc. Natl. Acad. Sci. U.S.A. 102 16678-83 PubMed
- ↑ Reid, BG et al. (2001) ClpA mediates directional translocation of substrate proteins into the ClpP protease. Proc. Natl. Acad. Sci. U.S.A. 98 3768-72 PubMed
- ↑ Engelberg-Kulka, H et al. (1998) rexB of bacteriophage lambda is an anti-cell death gene. Proc. Natl. Acad. Sci. U.S.A. 95 15481-6 PubMed
- ↑ Maxwell, KL et al. (2000) Thermodynamic and functional characterization of protein W from bacteriophage lambda. The three C-terminal residues are critical for activity. J. Biol. Chem. 275 18879-86 PubMed
- ↑ Weichart, D et al. (2003) Global role for ClpP-containing proteases in stationary-phase adaptation of Escherichia coli. J. Bacteriol. 185 115-25 PubMed
- ↑ Rajagopal, S et al. (2002) Sodium dodecyl sulfate hypersensitivity of clpP and clpB mutants of Escherichia coli. Appl. Environ. Microbiol. 68 4117-21 PubMed
- ↑ Kroh, HE & Simon, LD (1990) The ClpP component of Clp protease is the sigma 32-dependent heat shock protein F21.5. J. Bacteriol. 172 6026-34 PubMed
- ↑ Maurizi, MR et al. (1990) Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. J. Biol. Chem. 265 12536-45 PubMed
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