Clp Protease: Difference between revisions

From Proteopedia
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

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.[1]

For more details see

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 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.

E. coli Clp protease catalytic subunit (PDB entry 1tyf)

Drag the structure with the mouse to rotate

3D structures of Clp protease3D structures of Clp protease

Updated on 17-February-2019

ReferencesReferences

  1. 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky