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Clp Protease
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | CLP is a heterodimer containing an ATP-binding regulatory subunit A '''ClpA''' and catalytic subunit P '''ClpP'''. The proteolytic complex is composed of 2 heptameric rings of ClpP flanked by hexameric rings of ClpA. For full proteolytic activity ClpP must associate with one of two related ATPase subunits: ClpA and [[ClpX]]. | + | 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 2 heptameric rings of ClpP flanked by hexameric rings of ClpA. For full proteolytic activity ClpP must associate with one of two related ATPase subunits: ClpA and [[ClpX]]. |
</StructureSection> | </StructureSection> | ||
==3D structures of Clp protease== | ==3D structures of Clp protease== | ||
Revision as of 09:35, 31 January 2017
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3D structures of Clp protease
Updated on 31-January-2017
