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Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD

Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD

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KOVERMANN, Michael, Franz X SCHMID, Jochen BALBACH, 2013. Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD. In: Biological chemistry. 394(8), pp. 965-975. ISSN 1431-6730. eISSN 1437-4315. Available under: doi: 10.1515/hsz-2013-0137

@article{Kovermann2013-08Molec-44435, title={Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD}, year={2013}, doi={10.1515/hsz-2013-0137}, number={8}, volume={394}, issn={1431-6730}, journal={Biological chemistry}, pages={965--975}, author={Kovermann, Michael and Schmid, Franz X and Balbach, Jochen} }

eng Kovermann, Michael Schmid, Franz X Balbach, Jochen Schmid, Franz X SlyD is a bacterial two-domain protein that functions as a molecular chaperone, a prolyl cis/trans isomerase, and a nickel-binding protein. This review summarizes recent findings about the molecular enzyme mechanism of SlyD. The chaperone function located in one domain of SlyD is involved in twin-arginine translocation and increases the catalytic efficiency of the prolyl cis/trans isomerase domain in protein folding by two orders of magnitude. The C-terminal tail of SlyD binds Ni<sup>2+</sup> ions and supplies them for the maturation of [NiFe] hydrogenases. A combined biochemical and biophysical analysis revealed the molecular basis of the delicate interplay of the different domains of SlyD for optimal function. 2019-01-08T09:16:05Z Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD Balbach, Jochen 2013-08 2019-01-08T09:16:05Z Kovermann, Michael

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