Dynamic control of the prolyl isomerase function of the dual-domain SlyD protein

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2013
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Balbach, Jochen
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Biophysical Chemistry. 2013, 171, pp. 16-23. ISSN 0301-4622. eISSN 1873-4200. Available under: doi: 10.1016/j.bpc.2012.11.003
Zusammenfassung

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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Fachgebiet (DDC)
540 Chemie
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NMR, Fluorescence, PPIase, FKBP, Dynamics, Enzymology
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ISO 690KOVERMANN, 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.2012.11.003
BibTex
@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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