Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.6.1.7 extracted from

  • Zhang, J.; Baker, M.L.; Schroeder, G.F.; Douglas, N.R.; Reissmann, S.; Jakana, J.; Dougherty, M.; Fu, C.J.; Levitt, M.; Ludtke, S.J.; Frydman, J.; Chiu, W.
    Mechanism of folding chamber closure in a group II chaperonin (2010), Nature, 463, 379-383.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.1.7

Organism

Organism UniProt Comment Textmining
Methanococcus maripaludis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Methanococcus maripaludis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a folded polypeptide structures of a group II chaperonin in both open (nucleotide-free) and closed (ATP-induced) states at unprecedented resolutions by single particle cryo-EM and computational modeling reveals that in group II chaperonins the key structural rearrangements leading from the open to closed state are completely different from those found in group I chaperonins, despite structural similarities between the groups Methanococcus maripaludis ADP + phosphate + an unfolded polypeptide
-
 ?

Synonyms

Synonyms Comment Organism
Mm-cpn
-
 Methanococcus maripaludis