title: Proton nuclear magnetic resonance assignments and secondary structure determination of the ColE1 rop (rom) protein.
abstract: The complete resonance assignment of the ColE1 rop (rom) protein at pH 2.3 was obtained by two-dimensional (2D) proton nuclear magnetic resonance spectroscopy (1H NMR) at 500 and 600 MHz using through-bond and through-space connectivities. Sequential assignments and elements of regular secondary structure were deduced by analysis of nuclear Overhauser enhancement spectroscopy (NOESY) experiments and 3JHN alpha coupling constants. One 7.2-kDa monomer of the homodimer consists of two antiparallel helices connected by a hairpin loop at residue 31. The C-terminal peptide consisting of amino acids 59-63 shows no stable conformation. The dimer forms a four-helix bundle with opposite polarization of neighboring elements in agreement with the X-ray structure.
authors.affiliation: Department of Biophysics, Max-Planck-Institute for Medical Research, Heidelberg, FRG.
authors.forename: W
authors.initials: W
authors.lastname: Eberle
authors.forename: W
authors.initials: W
authors.lastname: Klaus
authors.forename: G
authors.initials: G
authors.lastname: Cesareni
authors.forename: C
authors.initials: C
authors.lastname: Sander
authors.forename: P
authors.initials: P
authors.lastname: Rösch
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D003087:Colicins; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010363:Pattern Recognition, Automated; D011487:Protein Conformation; D016601:RNA-Binding Proteins
chemical_list: D001426:Bacterial Proteins; D003087:Colicins; D016601:RNA-Binding Proteins; C054243:Rop protein, ColE1 plasmid; D006859:Hydrogen