Crystallization (Comment) | Organism |
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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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
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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 | UniProt | Comment | Textmining |
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Saccharolobus shibatae | - |
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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 | ? | - |
? |
Synonyms | Comment | Organism |
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archaeosome | - |
Saccharolobus shibatae |