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Literature summary for 3.6.4.B10 extracted from

  • Sekiguchi, H.; Nakagawa, A.; Moriya, K.; Makabe, K.; Ichiyanagi, K.; Nozawa, S.; Sato, T.; Adachi, S.; Kuwajima, K.; Yohda, M.; Sasaki, Y.C.
    ATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking (2013), PLoS ONE, 8, e64176.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.4.B10

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Thermococcus sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Thermococcus sp.
-
 ADP + phosphate
-
 ?
ATP + H2O Thermococcus sp. KS-1
-
 ADP + phosphate
-
 ?
additional information Thermococcus sp. ATP-dependent rotational motion of a group II chaperonin ?
-
 ?
additional information Thermococcus sp. KS-1 ATP-dependent rotational motion of a group II chaperonin ?
-
 ?

Organism

Organism UniProt Comment Textmining
Thermococcus sp. O24730 subunit beta
-
Thermococcus sp. P61112 subunit alpha
-
Thermococcus sp. KS-1 O24730 subunit beta
-
Thermococcus sp. KS-1 P61112 subunit alpha
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
 Thermococcus sp. ADP + phosphate
-
 ?
ATP + H2O
-
 Thermococcus sp. KS-1 ADP + phosphate
-
 ?
additional information ATP-dependent rotational motion of a group II chaperonin Thermococcus sp. ?
-
 ?
additional information ATP-dependent rotational motion of a group II chaperonin Thermococcus sp. KS-1 ?
-
 ?

Synonyms

Synonyms Comment Organism
TKS1-CPN
-
 Thermococcus sp.

General Information

General Information Comment Organism
evolution the enzyme belongs to the group II chaperonins, that play important roles in protein homeostasis in the eukaryotic cytosol and in Archaea Thermococcus sp.
additional information determination of ATP-dependent dynamics of a group II chaperonin at the single-molecule level with highly accurate rotational axes views by UV light-triggered diffracted X-ray tracking, using caged-ATP and stopped-flow fluorometry. The closed ring twists counterclockwise and the twisted ring reverted to the original open-state with a clockwise motion, the biphasic lid-closure process occurs with unsynchronized closure and a synchronized counterclockwise twisting motion Thermococcus sp.
physiological function group II chaperonin proteins assist in the folding of nascent polypeptides and also refold unfolded proteins in an ATP-dependent manner. Chaperonin-mediated protein folding is dependent on the closure and opening of a built-in lid, which is controlled by the ATP hydrolysis cycle Thermococcus sp.