Clp Protease: Difference between revisions
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* [[Molecular Playground/ClpP]] | * [[Molecular Playground/ClpP]] | ||
* [[Molecular Playground/E. coli ClpP]]. | * [[Molecular Playground/E. coli ClpP]]. | ||
'''Clp'''X or '''ATP-dependent Clp protease ATP-binding subunit ClpX''' is a molecular chaperone which alters the shape of DNA during bacteriophage μ transposition.<ref>PMID:21736903</ref> For details see [[Molecular Playground/Hexameric ClpX]] | |||
== Structural highlights == | == Structural highlights == | ||
CLP is a heterodimer containing an ATP-binding regulatory subunit A '''ClpA''' or Hsp100 in [[Heat Shock Proteins]] and catalytic subunit P '''ClpP'''. The proteolytic complex is composed of <scene name='50/508398/Cv/2'>2 heptameric rings of ClpP</scene> flanked by hexameric rings of ClpA. For full proteolytic activity ClpP must associate with one of two related ATPase subunits: ClpA and | CLP is a heterodimer containing an ATP-binding regulatory subunit A '''ClpA''' or Hsp100 in [[Heat Shock Proteins]] and catalytic subunit P '''ClpP'''. The proteolytic complex is composed of <scene name='50/508398/Cv/2'>2 heptameric rings of ClpP</scene> flanked by hexameric rings of ClpA. For full proteolytic activity ClpP must associate with one of two related ATPase subunits: '''ClpA''' and '''ClpX''' or '''ATP-binding Clp protease ATP-binding subunit ClpX'''. | ||
==3D structures of Clp protease== | ==3D structures of Clp protease== | ||
Revision as of 13:47, 24 November 2022
FunctionClp protease (CLP) is a serine peptidase which hydrolyzes proteins in the presence of ATP and Mg+2 ion. CLP is found in mitochondria. CLP participates in degradation of misfolded proteins.[1] For more details see ClpX or ATP-dependent Clp protease ATP-binding subunit ClpX is a molecular chaperone which alters the shape of DNA during bacteriophage μ transposition.[2] For details see Molecular Playground/Hexameric ClpX Structural highlightsCLP is a heterodimer containing an ATP-binding regulatory subunit A ClpA or Hsp100 in Heat Shock Proteins and catalytic subunit P ClpP. The proteolytic complex is composed of flanked by hexameric rings of ClpA. For full proteolytic activity ClpP must associate with one of two related ATPase subunits: ClpA and ClpX or ATP-binding Clp protease ATP-binding subunit ClpX. 3D structures of Clp protease
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ReferencesReferences
- ↑ Maurizi MR, Clark WP, Katayama Y, Rudikoff S, Pumphrey J, Bowers B, Gottesman S. Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. J Biol Chem. 1990 Jul 25;265(21):12536-45. PMID:2197275
- ↑ Baker TA, Sauer RT. ClpXP, an ATP-powered unfolding and protein-degradation machine. Biochim Biophys Acta. 2012 Jan;1823(1):15-28. doi: 10.1016/j.bbamcr.2011.06.007. , Epub 2011 Jun 27. PMID:21736903 doi:http://dx.doi.org/10.1016/j.bbamcr.2011.06.007