Clp Protease: Difference between revisions
Michal Harel (talk | contribs) New page: '''Clp 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 misfolde... |
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<StructureSection load='1tyf' size='350' side='right' caption='E. coli Clp protease catalytic subunit (PDB entry [[1tyf]])' scene='50/508398/Cv/1'> | |||
''' | == Function == | ||
'''Clp 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.<ref>PMID:2197275</ref><br /> | |||
For more details see <br /> | |||
* [[Clp protease]] | |||
* [[Zinc Fingers]] | |||
* [[Molecular Playground/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 == | |||
[[ | 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'''. | ||
= | <scene name='45/458468/Cv/4'>ADP binding site</scene> in ''Helicobacter pylori'' ClpX (PDB entry [[1um8]]).<ref>PMID:14514695</ref> | ||
==3D structures of Clp protease== | |||
[[Clp protease 3D structures]] | |||
[[ | |||
</StructureSection> | |||
[[ | == References == | ||
<references/> | |||
[[Category:Topic Page]] |