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• W1991887913 abstract "Significance Molecular machines, such as the proteasome in eukaryotes and archaea as well as the HslU–HslV complex in bacteria, play critical roles in maintaining cellular homeostasis. Here, we have used methyl-Transverse Relaxation-Optimized Spectroscopy to study the 230 kDa HslV dodecamer that cleaves substrate polypeptides. The initial catalytic step is investigated by measuring the pK a of the terminal amine of catalytic residue T1. Furthermore, we show that single site mutations in key regions, which contact HslU or change on HslU binding, lead to propagated changes in structure along an allosteric pathway, affecting proteolysis rates. NMR relaxation experiments are consistent with a coupling of millisecond timescale dynamics throughout regions of HslV that link HslU and substrate binding with catalysis." @default.
• W1991887913 created "2016-06-24" @default.
• W1991887913 creator A5020050875 @default.
• W1991887913 creator A5082192358 @default.
• W1991887913 date "2014-01-27" @default.
• W1991887913 modified "2023-10-18" @default.
• W1991887913 title "Tracing an allosteric pathway regulating the activity of the HslV protease" @default.
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• W1991887913 doi "https://doi.org/10.1073/pnas.1318476111" @default.
• W1991887913 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3926032" @default.
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