This change directly impacts the placement of the catalytic triad residues (Ser-153, His-178, and Asp-227) in the active site. The His-178 ring separates from Ser-153 by more than 5 Å, while rotating by about 70°. Asp-227 moves 2.8 Å in the same direction (Figure S3F). ...
In the EcClpP+ACP1-06 structure, we found an unexplained electron density in all 14 subunits extending from the nucleophilic residue S111 of the catalytic triad, suggesting a covalent modification (Supplementary Fig.1a, b). The density extends at approximately right angles in opposite directions a...
Like bacterial ClpP, mitochondrial ClpP also has three different conformational states: extended, compacted, and compressed. Among them, only the extended form demonstrates catalytic activity required for substrate degradation, while the others are assumed to be part of a barrel-opening cycle2,33,34,...
(MSA), central ClpP sequence features such as the Ser-His-Asp catalytic triad26,27,28as well as the putative oligomeric state Asp/Arg sensor are conserved in ctClpP1 and ctClpP2. Notably, however, while the N-terminal region including the chaperone binding motif29is highly conserved in ...
We find that ADEPs are able to revert the catalytically incompetent compressed conformation of the D172N ClpP mutant through switching its conformation to the extended state, which exhibits an aligned catalytic triad (contrary to the compressed conformation, where the triad is not aligned). Similarly...
Another accepted ClpP peptidase inhibitor, β-lactones, bind specifically to the SauClpP catalytic triad to abolish the activity of the SauClpP; however, it fails to abolish in the presence of the ADEP analog (ADEP7) [31]. It is suggested that a total of seven to fourteen ADEP molecule ...
(catalytic nucleophile)酪氨酸(Tyr63,Y)为高度保守的催化三 分体残基(catalytic triad residues),在酪蛋白水解中发挥重要 作用8。此外,PlclpP 序列还含有丝氨酸蛋白水解酶高度保守的催化 活性位点(Ser99-His124-Asp173)(图1)。基因表达质粒pET-28a- PlclpP 的构建与鉴定基于本研究获得的PlclpP 基因序列,设计了携...
We find that ADEPs are able to revert the catalytically incompetent compressed conformation of the D172N ClpP mutant through switching its conformation to the extended state, which exhibits an aligned catalytic triad (contrary to the compressed conformation, where the triad is not aligned). Similarly...
suggesting that the flexible N-terminal extremity of mycobacterial ClpPs participated in the destabilization of interaction between heptamers./p pConclusion/p pDespite the conservation of a Ser protease catalytic triad in their primary sequences, mycobacterial ClpP1 and ClpP2 do not have conventional ...