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

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2013

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Schmid, Franz X
Balbach, Jochen

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http://nbn-resolving.de/urn:nbn:de:bsz:352-2-15ght4w1yj8wg9
DOI (zitierfähiger Link)
https://doi.org/10.1515/hsz-2013-0137
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Chemie: Publikationen
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Published

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Biological chemistry. 2013, 394(8), pp. 965-975. ISSN 1431-6730. eISSN 1437-4315. Available under: doi: 10.1515/hsz-2013-0137

Zusammenfassung

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 Ni2+ 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.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
540 Chemie

Schlagwörter

chaperone; enzyme mechanism; nickel metalloprotein; protein folding; prolyl isomerase

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ISO 690KOVERMANN, Michael, Franz X SCHMID, Jochen BALBACH, 2013. Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD. In: Biological chemistry. 2013, 394(8), pp. 965-975. ISSN 1431-6730. eISSN 1437-4315. Available under: doi: 10.1515/hsz-2013-0137
BibTex
@article{Kovermann2013-08Molec-44435,
  year={2013},
  doi={10.1515/hsz-2013-0137},
  title={Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD},
  number={8},
  volume={394},
  issn={1431-6730},
  journal={Biological chemistry},
  pages={965--975},
  author={Kovermann, Michael and Schmid, Franz X and Balbach, Jochen}
}
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