title: Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD.
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.
authors.affiliation: Institut für Physik, Biophysik, und Mitteldeutsches Zentrum für Struktur und Dynamik der Proteine MZP, Martin-Luther Universität Halle-Wittenberg, D-06120 Halle, Germany.
authors.forename: Michael
authors.initials: M
authors.lastname: Kovermann
authors.forename: Franz X
authors.initials: FX
authors.lastname: Schmid
authors.forename: Jochen
authors.initials: J
authors.lastname: Balbach
mesh_terms: D001419:Bacteria / Q000737:chemistry* / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D056511:Metallochaperones / Q000737:chemistry / Q000378:metabolism; D008968:Molecular Conformation; D019696:Peptidylprolyl Isomerase / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D001426:Bacterial Proteins; D056511:Metallochaperones; D019696:Peptidylprolyl Isomerase