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

Title data

Kovermann, Michael ; Schmid, Franz X. ; Balbach, Jochen:
Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD.
In: Biological Chemistry. Vol. 394 (August 2013) Issue 8 . - pp. 965-975.
ISSN 1431-6730
DOI: https://doi.org/10.1515/hsz-2013-0137

Abstract in another language

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.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 23585180
Institutions of the University: Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Professorship Biochemistry - Univ.-Prof. Dr. Franz Xaver Schmid
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Professorship Biochemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 21 Apr 2015 13:46
Last Modified: 08 Feb 2016 08:35
URI: https://eref.uni-bayreuth.de/id/eprint/10536