Publikation: Dynamic control of the prolyl isomerase function of the dual-domain SlyD protein
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Local dynamics on variable timescales are important to facilitate high catalytic efficiency in enzymes. In this study, we examined the dual-domain peptidyl-prolyl cis/trans-isomerase (PPIase) SlyD with regard to its catalytic cycle. Fluorescence- and NMR-based experiments were performed to understand the high catalytic efficiency of SlyD compared to single domain FKBP proteins. We probed local conformational changes for amino acids involved in substrate-binding (IF domain) and substrate-catalysis (FKBP domain) taking place on the timescale of substrate turnover. Binding of the PPIase activity inhibitors to the FKBP domain suppressed the conformational freedom of the remote IF domain. A single side-chain mutation in the active site strongly reduced the rate of substrate turnover and changed the conformational dynamics of all amino acids involved in catalysis. This dynamic interplay between substrate-binding domain and PPIase domain determines the high catalytic activity of SlyD and inhibitor-binding modulates the backbone plasticity required for enzyme activity.
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KOVERMANN, Michael, Jochen BALBACH, 2013. Dynamic control of the prolyl isomerase function of the dual-domain SlyD protein. In: Biophysical Chemistry. 2013, 171, pp. 16-23. ISSN 0301-4622. eISSN 1873-4200. Available under: doi: 10.1016/j.bpc.2012.11.003BibTex
@article{Kovermann2013-01Dynam-44410, year={2013}, doi={10.1016/j.bpc.2012.11.003}, title={Dynamic control of the prolyl isomerase function of the dual-domain SlyD protein}, volume={171}, issn={0301-4622}, journal={Biophysical Chemistry}, pages={16--23}, author={Kovermann, Michael and Balbach, Jochen} }
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