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Q41063926-097BBB7E-699E-4E38-A32C-CEA82DF51CE6
Q41063926-097BBB7E-699E-4E38-A32C-CEA82DF51CE6
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Statement
http://www.wikidata.org/entity/statement/Q41063926-097BBB7E-699E-4E38-A32C-CEA82DF51CE6
Control of substrate gating and translocation into ClpP by channel residues and ClpX binding.
P2860
Q41063926-097BBB7E-699E-4E38-A32C-CEA82DF51CE6
BestRank
Statement
http://www.wikidata.org/entity/statement/Q41063926-097BBB7E-699E-4E38-A32C-CEA82DF51CE6
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wasDerivedFrom
b18b26d56e5fde2bd8b59cabef7356a3d24b96e9
P2860
The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation.