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Literature summary for 5.6.1.7 extracted from

  • Quaite-Randall, E.; Trent, J.D.; Josephs, R.; Joachimiak, A.
    Conformational cycle of the archaeosome, a TCP1-like chaperonin from Sulfolobus shibatae (1995), J. Biol. Chem., 270, 28818-28823.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
electron microscopy and circular dichroism study reveal two distinct conformational states that are part of chaperonin functional cycle. The closed archaeosome complex binds ATP and forms an open complex. Upon ATP hydrolysis, the open complex dissociates into subunits. Free subunits reassemble into a two-ring structure Saccharolobus shibatae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharolobus shibatae enzyme has two distinct conformational states that are part of chaperonin functional cycle. The closed archaeosome complex binds ATP and forms an open complex. Upon ATP hydrolysis, the open complex dissociates into subunits. Free subunits reassemble into a two-ring structure. Denatured proteins associate with both conformational states as well as with free subunits that form an intermediate complex ?
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Organism

Organism UniProt Comment Textmining
Saccharolobus shibatae
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme has two distinct conformational states that are part of chaperonin functional cycle. The closed archaeosome complex binds ATP and forms an open complex. Upon ATP hydrolysis, the open complex dissociates into subunits. Free subunits reassemble into a two-ring structure. Denatured proteins associate with both conformational states as well as with free subunits that form an intermediate complex Saccharolobus shibatae ?
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?

Synonyms

Synonyms Comment Organism
archaeosome
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Saccharolobus shibatae