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- cpn60_chaperonin_family abstract "TCP-1/cpn60 chaperonin family is a family of evolutionarily related proteins.This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family. The assembly of proteins has been thought to be the sole result of properties inherent in the primary sequence of polypeptides themselves. In some cases, however, structural information from other protein molecules is required for correct folding and subsequent assembly into oligomers. These 'helper' molecules are referred to as molecular chaperones, a subfamily of which are the chaperonins, which include 10 kDa and 60 kDa proteins. These are found in abundance in prokaryotes, chloroplasts and mitochondria. They are required for normal cell growth (as demonstrated by the fact that no temperature sensitive mutants for the chaperonin genes can be found in the temperature range 20 to 43 degrees Celsius) and are stress-induced, acting to stabilise or protect disassembled polypeptides under heat-shock conditions.The 10 kDa chaperonin (cpn10 - or groES in bacteria) exists as a ring-shaped oligomer of between 6 to 8 identical subunits, whereas the 60 kDa chaperonin (cpn60 - or groEL in bacteria) forms a structure comprising 2 stacked rings, each ring containing 7 identical subunits. These ring structures assemble by self-stimulation in the presence of Mg2+-ATP. The cpn10 and cpn60 oligomers also require Mg2+-ATP in order to interact to form a functional complex, although the mechanism of this interaction is as yet unknown. This chaperonin complex is essential for the correct folding and assembly of polypeptides into oligomeric structures, of which the chaperonins themselves are not a part. The binding of cpn10 to cpn60 inhibits the weak ATPase activity of cpn60.The 60 kDa form of chaperonin is the immunodominant antigen of patients with Legionnaire's disease, and is thought to play a role in the protection of the Legionella bacteria from oxygen radicals within macrophages. This hypothesis is based on the finding that the cpn60 gene is upregulated in response to hydrogen peroxide, a source of oxygen radicals. Cpn60 has also been found to display strong antigenicity in many bacterial species and has the potential for inducing immune protection against unrelated bacterial infections. The RuBisCO subunit binding protein (which has been implicated in the assembly of RuBisCO) and cpn60 have been found to be evolutionary homologues, the RuBisCO subunit binding protein having the C-terminal Gly-Gly-Met repeat found in all bacterial cpn60 sequences. Although the precise function of this repeat is unknown, it is thought to be important as it is also found in 70 kDa heat-shock proteins. The crystal structure of Escherichia coli GroEL has been resolved to 2.8 Å. The TCP-1 family of proteins act as molecular chaperones for tubulin, actin and probably some other proteins. They are weakly, but significantly, related to the cpn60/groEL chaperonin family.".
- cpn60_chaperonin_family symbol "Cpn60_TCP1".
- cpn60_chaperonin_family thumbnail PDB_1grl_EBI.jpg?width=300.
- cpn60_chaperonin_family wikiPageID "27920001".
- cpn60_chaperonin_family wikiPageRevisionID "593131339".
- cpn60_chaperonin_family caption "Structure of the bacterial chaperonin GroEL.".
- cpn60_chaperonin_family cdd "cd03333".
- cpn60_chaperonin_family hasPhotoCollection cpn60_chaperonin_family.
- cpn60_chaperonin_family interpro "IPR002423".
- cpn60_chaperonin_family name "TCP-1/cpn60 chaperonin family".
- cpn60_chaperonin_family pdb "K:23-525 Z:23-525 A:190-375 H:23-525 F:23-525 E:23-525 J:23-524 J:23-524 I:23-525 J:23-524 K:23-525 C:190-335 L:23-525 E:23-524 H:23-525 H:23-525 E:23-524 :190-375 F:23-525 B:23-524 A:190-375 A:190-335 :190-335 A:187-378 A:23-526 e:22-526 E:22-526 B:42-522 A:1-143 B:33-521 B:33-521 B:215-366 :214-364 :214-364 H:210-380 B:210-380".
- cpn60_chaperonin_family pfam "PF00118".
- cpn60_chaperonin_family prosite "PDOC00610".
- cpn60_chaperonin_family scop "1".
- cpn60_chaperonin_family symbol "Cpn60_TCP1".
- cpn60_chaperonin_family subject Category:Protein_domains.
- cpn60_chaperonin_family type Biomolecule.
- cpn60_chaperonin_family type Protein.
- cpn60_chaperonin_family type BiologicalObject.
- cpn60_chaperonin_family comment "TCP-1/cpn60 chaperonin family is a family of evolutionarily related proteins.This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family. The assembly of proteins has been thought to be the sole result of properties inherent in the primary sequence of polypeptides themselves.".
- cpn60_chaperonin_family label "TCP-1/cpn60 chaperonin family".
- cpn60_chaperonin_family sameAs m.0ch1nd1.
- cpn60_chaperonin_family sameAs Q7669740.
- cpn60_chaperonin_family sameAs Q7669740.
- cpn60_chaperonin_family wasDerivedFrom cpn60_chaperonin_family?oldid=593131339.
- cpn60_chaperonin_family depiction PDB_1grl_EBI.jpg.
- cpn60_chaperonin_family isPrimaryTopicOf cpn60_chaperonin_family.
