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Literature summary for 3.4.21.92 extracted from

  • Gersch, M.; Famulla, K.; Dahmen, M.; Goebl, C.; Malik, I.; Richter, K.; Korotkov, V.S.; Sass, P.; Ruebsamen-Schaeff, H.; Madl, T.; Broetz-Oesterhelt, H.; Sieber, S.A.
    AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control (2015), Nat. Commun., 6, 6320.
    View publication on PubMed
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Activating Compound

Activating Compound Comment Organism Structure
acyldepsipeptide acyldepsipeptides in addition to opening the axial pore directly stimulate ClpP activity through cooperative binding Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus Q2G036
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Staphylococcus aureus NCTC 8325 Q2G036
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General Information

General Information Comment Organism
physiological function both protein and small-molecule activators of ClpP allosterically control the ClpP barrel conformation. Acyldepsipeptides in addition to opening the axial pore directly stimulate ClpP activity through cooperative binding. ClpP activation thus reaches beyond active site accessibility and also involves conformational control of the catalytic residues. Substoichiometric amounts of acyldepsipeptide potently prevent binding of ClpX to ClpP and, at the same time, partially inhibit ClpP through conformational perturbance. The hydrophobic binding pocket is a major conformational regulatory site with implications for both ClpXP proteolysis and acyldepsipeptide -based anti-bacterial activity Staphylococcus aureus