ClpX
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| CLPX | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Aliases | CLPX, ClpX, caseinolytic mitochondrial matrix peptidase chaperone subunit, EPP2, caseinolytic mitochondrial matrix peptidase chaperone subunit X | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 615611; MGI: 1346017; HomoloGene: 4851; GeneCards: CLPX; OMA:CLPX - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial is an enzyme that in humans is encoded by the CLPX gene. This protein is a member of the family of AAA Proteins (AAA+ ATPase) and is to form the protein complex of Clp protease (Endopeptidase Clp).
Tertiary
The human enzyme ClpX is drawn from the protein complex structure of Clp protease. These hexameric HSP100/Clp proteins produce ring like structures resembling chaperonins.[5]
The Clp proteases have a two-component structure which includes two different proteolytic cores and multiple chaperone rings. As a result, there are several possible combinations of Clp protease complexes. The ClpP protease core can partner with different chaperones, namely ClpA, ClpC, ClpE, and ClpX, to form active chaperone-protease complexes. On the other hand, ClpQ interacts exclusively with the ClpY chaperone to form the ClpYQ protease (also called HslUV) . The Clp-type ATPases can be classified into two distinct groups: class I with two consecutive AAA modules per protomer(ClpA, ClpC, and ClpE) and class II with only one AAA module per protomer.[6]
ClpA and ClpX of E. coli are protein unfoldases that require ATP to function. They individually associate with the ClpP protease to facilitate targeted protein degradation.[7] These variants have inflicted variants interspecific with ClpP.
Quaternary
The complex assembly of the regulatory subunits of ATP-dependent Clp proteases is induced in the critical role in cellular thermotolerance. There are numerous proteases that are thought to have a bacterial origin. Studies on the protein of E. coli are the main source of information about the human ClpX protein. In E. coli, the ClpX protein monomer has an N-terminal domain and a AAA+ module made up of two AAA+ domains, one larger than the other.[8] Since the prevalence of E.coli is at such a high factor in most people around the world, the constitutive aspect of ClpX showed multiple signs in research of the protease.
Clp protease is made up of ATPase-active chaperone rings and a proteolytic core, two functional units with distinct functions that play a role in cellular thermotolerance.[9][10] The ClpXP chaperone-protease is present in almost every type of bacteria, commonly found together with the widely distributed Lon and FtsH proteases. Hence, ClpXP is the most prevalent among the Clp.[11]
The HslV rings engage with an unrelated chaperone ATPase called HslU, which also has 6-fold ring symmetry. This is similar to the ClpX chaperone, which it potentially evolved from, and almost all AAA+ ATPase proteins that emerged from a surge of gene duplications prior to the last common ancestor of all life. This allows the assumption that most mammals from the common ancestors between humans and mice were shown to have this relating enzyme. As shown on the infobox gene similarity between a mouse and a human, we can distinctly see its similarities and differences in the Clp protease.
