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== | ||