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Updated: May 12, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD
Michael Kovermann1, Franz X Schmid, Jochen Balbach
1Institut für Physik, Biophysik, und Mitteldeutsches Zentrum für Struktur und Dynamik der Proteine MZP, Martin-Luther Universität Halle-Wittenberg, D-06120 Halle, Germany.
Abstract:
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.
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