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Literature summary for 5.6.1.7 extracted from

  • Douglas, N.R.; Reissmann, S.; Zhang, J.; Chen, B.; Jakana, J.; Kumar, R.; Chiu, W.; Frydman, J.
    Dual action of ATP hydrolysis couples lid closure to substrate release into the group II chaperonin chamber (2011), Cell, 144, 240-252.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.1.7

Protein Variants

Protein Variants Comment Organism
additional information a lid variant is created that lacks the entire lid-forming segments: variant achieves the same ATP-induced closed conformation as wild-type, ATPase activity and substrate-binding ability are unaffected, substrate release from mutant cannot be ascribed to completion of folding Methanococcus maripaludis
T327A/N328A/K330A/D331A mutants achieve essentially the same closed state as the wild-type counterparts, mutants are competent for ATP binding and hydrolysis. Another mutant which in addition to the 4 Ala substitution lacks the entire lid-forming segments is incapable of releasing either substrate in the presence of ATP. This suggests that the lateral contacts between helix 11 and the rls loop 327-331 are important for releasing the substrate upon ATP hydrolysis Methanococcus maripaludis

Organism

Organism UniProt Comment Textmining
Methanococcus maripaludis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a folded polypeptide ATP hydrolysis has a dual role in group II chaperonin function, promoting both lid closure and release of the substrate into the cavity. Importantly, both events must occur for successful substrate folding. An alternate model for group II chaperonin function is suggested, whereby folding relies on the release of the substrate into a unique chemical environment within the closed chamber Methanococcus maripaludis ADP + phosphate + an unfolded polypeptide
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Synonyms

Synonyms Comment Organism
CPN
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 Methanococcus maripaludis
group II chaperonin
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 Methanococcus maripaludis