NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain of the trigger factor from Mycoplasma genitalium compared to FK506-binding protein.

We have solved the solution structure of the peptidyl-prolyl cis-trans isomerase (PPIase) domain of the trigger factor from Mycoplasma genitalium by homo- and heteronuclear NMR spectroscopy. Our results lead to a well-defined structure with a backbone rmsd of 0.23 A.

Regioselective Cleavage by a Palladium(II) Aqua Complex of a Polypeptide in Different Overall Conformations.

Two molecules of the complex cis-[Pd(en)(H(2)O)(2)](2+) lose aqua ligands and bind to His5 and His9 residues in the nonadecapeptide that is the carboxy-terminal segment of the protein myohemerythrin. The known modes of palladium(II)-histidine coordination are detected by (1)H NMR spectroscopy. Only the [Pd(en)(H(2)O)](2+)group bound to His5 cleaves the polypeptide backbone; the group bound to His9 does not.