Two-dimensional 1H nuclear magnetic resonance studies on the gene V-encoded single-stranded DNA-binding protein of the filamentous bacteriophage IKe. I. Structure elucidation of the DNA-binding wing.

摘要: Two-dimensional nuclear magnetic resonance techniques were used to obtain residue- and sequence-specific assignments in the 1H spectrum of single-stranded DNA-binding protein encoded by gene V filamentous phage IKe (IKe GVP). The residue-specific are based on analysis J-correlated spectra, i.e. correlated spectroscopy homonuclear-Hartmann-Hahn total spectroscopy. Complete side-chain spin systems, e.g. long side-chains, were, a major part, derived from two-dimensional spectra obtained means latter technique. Sequence-specific residue for two neighbouring residues V41 Y42, amino acid sequence segment encompassing S17 through I29. The structure this segment, β-loop, was deduced interresidue Overhauser effect pattern. Residues V19 P26 I29 form an anti-parallel β-ladder whereas Q21 K25 constitute loop region. β-loop is expected project into solution intimately involved binding DNA; it therefore designated “DNA-binding wing”. By analogy with wing GVP, similar proposed corresponding domain Ff which, X-ray diffraction studies, three-dimensional has been deduced. Essential differences appear exist between that paper. Possible reasons these discussed.