Clp Protease: Difference between revisions
Jump to navigation
Jump to search
Michal Harel (talk | contribs) No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
<StructureSection load='1tyf' size='350' side='right' caption='E. coli Clp protease catalytic subunit (PDB entry [[1tyf]])' scene=''> | <StructureSection load='1tyf' size='350' side='right' caption='E. coli Clp protease catalytic subunit (PDB entry [[1tyf]])' scene='50/508398/Cv/1'> | ||
== Function == | == Function == | ||
Revision as of 13:55, 17 February 2019
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 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 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. |
|
3D structures of Clp protease3D structures of Clp protease
Updated on 17-February-2019