Molecular Playground/E. coli ClpP: Difference between revisions
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== ClpP Introduction == | == ClpP Introduction == | ||
''E. coli'' Casein lytic proteinase P (ClpP) is a double ring [http://en.wiktionary.org/wiki/tetradecamer tetradecameric] homo oligomer compartmentalized peptidase [http://www.ncbi.nlm.nih.gov/pubmed/?term=ClpP%3A+A+structurally+dynamic+protease+regulated+by+AAA%2B+proteins]. ClpP requires the use of ATP dependent regulatory elements that independently bind to ClpP in order for substrates to have access the active core [http://www.ncbi.nlm.nih.gov/pubmed/15037252][http://www.ncbi.nlm.nih.gov/pubmed/20236930][http://www.ncbi.nlm.nih.gov/pubmed/19038348]. Here, proteins that are translocated by regulatory elements into the peptidase core are cleaved into smaller amino acid chains approximately on average 6-8aa in length [http://www.ncbi.nlm.nih.gov/pubmed/16229481]. | ''E. coli'' Casein lytic proteinase P (<scene name='60/609790/Clpp-2/2'>ClpP</scene>) is a double ring [http://en.wiktionary.org/wiki/tetradecamer tetradecameric] homo oligomer compartmentalized peptidase [http://www.ncbi.nlm.nih.gov/pubmed/?term=ClpP%3A+A+structurally+dynamic+protease+regulated+by+AAA%2B+proteins]. ClpP requires the use of ATP dependent regulatory elements that independently bind to ClpP in order for substrates to have access the active core [http://www.ncbi.nlm.nih.gov/pubmed/15037252][http://www.ncbi.nlm.nih.gov/pubmed/20236930][http://www.ncbi.nlm.nih.gov/pubmed/19038348]. Here, proteins that are translocated by regulatory elements into the peptidase core are cleaved into smaller amino acid chains approximately on average 6-8aa in length [http://www.ncbi.nlm.nih.gov/pubmed/16229481]. | ||
== Tetradecameric Structure == | == Tetradecameric Structure == | ||
ClpP is a serine protease which consists of fourteen monomers situated into two [http://en.wiktionary.org/wiki/heptamer heptameric] rings seated on top of each other. In the center of the barrel-shaped chamber lies a core of fourteen peptide-cleaving active sites, restricted by the narrow entrance called the <scene name='60/609790/Clpp_axial_pore/4'>axial pore</scene>. As peptides are [http://en.wikipedia.org/wiki/Processivity processively] threaded in the pore by the regulatory elements, the peptides are then degraded into smaller fragments as a result from ClpP cleavage. Smaller peptides are then released through small openings found around the <scene name='60/609790/Clpp_equator_pore/2'>equatorial interface</scene> of the two stacked rings. | ClpP is a serine protease which consists of fourteen monomers situated into two [http://en.wiktionary.org/wiki/heptamer heptameric] rings seated on top of each other. In the center of the barrel-shaped chamber lies a core of fourteen peptide-cleaving active sites, restricted by the narrow entrance called the <scene name='60/609790/Clpp_axial_pore/4'>axial pore</scene>. As peptides are [http://en.wikipedia.org/wiki/Processivity processively] threaded in the pore by the regulatory elements, the peptides are then degraded into smaller fragments as a result from ClpP cleavage. Smaller peptides are then released through small openings found around the <scene name='60/609790/Clpp_equator_pore/2'>equatorial interface</scene> of the two stacked rings. | ||
