EC Number   |
Reference |
|---|
   3.4.21.92 | - |
653260 |
| 3.4.21.92 | by the microbatch method at 14°C. Crystal structure of ClpP, at a resolution of 2.6 A, in complex with product peptides (heptapeptide) bound to the active site as well as in the apo state and crystal structure of the ClpP mutant, at 2.5 A resolution, and in complex with a tetrapeptide. In the complex structure, the peptides are zipped with two antiparallel strands of ClpP and point to the adjacent active site, explaining the broad substrate specificity, the product inhibition and the processive degradation of substrates in the chamber. Substrate binding causes local conformational changes around the active site that ultimately induce the active conformation of ClpP. The peptide binds to the active site of ClpP via hydrogen-bond networks |
699539 |
| 3.4.21.92 | ClpP structures have been solved from five different organisms |
683473 |
| 3.4.21.92 | ClpP structures have been solved from five different organisms, human ClpP can form a complex with Escherichia coli ClpX in vitro |
683473 |
| 3.4.21.92 | cryoelectron microscopy at 11 A resolution is used to visualize ClpAP (AAA+ ATPase/unfoldase), aiming to gain insight into ClpP as complexed with ClpA and the structural changes that their interaction may entail. The availability of crystal structures for ClpP that could be fitted into the cryoelectron microscopy density maps shows its changes in conformation that accompany binding of ClpA |
717787 |
| 3.4.21.92 | crystal structure of ClpP from Bacillus subtilis shows a significantly compressed shape along the axial direction. A portion of the handle regions comprising the heptameric ring-ring contacts shows structural transition from an ordered to a disordered state, which triggers the large conformational change from an extended to an overall compressed structure. Along with this structural change, 14 side pores are generated for product release and the catalytic triad adopts an inactive orientation |
718114 |
| 3.4.21.92 | modeling of chaperone ClpC and ClpP3/R subunit structures. The R-ring of ClpP3 is most likely to associate with ClpC |
731272 |
| 3.4.21.92 | mutant A153P, disruption of handle region resulting in an altered ring-ring dimerization interface. There exists a flexible N-terminal loop in each enzyme subunit that is important for complex formation with ClpXP and ClpAP |
669324 |
| 3.4.21.92 | mutant Y63A displays promoted self-activated proteolysis, which is a result of an enlarged entrance pore |
752359 |
| 3.4.21.92 | SaClpP consists of two heptameric rings that form a tetradecameric barrel. Compared to other ClpP structures, the barrel is compressed by roughly 10 A along the axial direction, and the ring-ring interface contains 14 equatorial side pores that can be up to 6 A in diameter, depending on the side-chain conformations. The side pores are lined with conserved hydrophobic residues and apparently represent the long-sought exit route for peptide products from the barrel chamber |
717089 |
