Structure of the DNA binding wing of the gene‐V encoded single‐stranded DNA binding protein of the filamentous bacteriophage M13
- 12 February 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 261 (1) , 1-4
- https://doi.org/10.1016/0014-5793(90)80621-o
Abstract
The structure in solution of a β-loop in mutant Y41H of the single-stranded DNA binding protein encoded by gene-V of the filamentous phage M13 has been elucidated using 2-dimensional 1H-nuclear magnetic resonance techniques. Furthermore, these studies enabled us to demonstrate that an identical structural element is present in wild-type gene-V-protein and that this element intimately is involved in the binding of gene-V-protein to single-stranded DNA. It is shown that the structure of the DNA binding wing deviates from that proposed for the same amino acid sequence on the basis of X-ray diffraction data. The structure is, however, identical to that of the DNA binding wing present in the single-stranded DNA binding protein encoded by the genome of the evolutionary distantly related filamentous phage IKe. The latter observations support our current view that in the binding of these proteins to single-stranded DNA a common structural motif is involved.Keywords
This publication has 17 references indexed in Scilit:
- Two-dimensional 1H nuclear magnetic resonance studies on the gene V-encoded single-stranded DNA-binding protein of the filamentous bacteriophage IKe: II. Characterization of the DNA-binding wing with the aid of spin-labelled oligonucleotidesJournal of Molecular Biology, 1989
- 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 wingJournal of Molecular Biology, 1989
- Water suppression in two-dimensional spin-locked NMR experiments using a novel phase-cycling procedureJournal of the American Chemical Society, 1987
- Two-dimensional proton NMR of gene 5 protein indicates that only two aromatic rings interact significantly with oligodeoxynucleotide basesBiochemistry, 1987
- MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopyJournal of Magnetic Resonance (1969), 1985
- Improved spectral resolution in COSY 1H NMR spectra of proteins via double quantum filteringBiochemical and Biophysical Research Communications, 1983
- Refined structure of the gene 5 DNA binding protein from bacteriophage fdJournal of Molecular Biology, 1983
- Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteinsBiochemical and Biophysical Research Communications, 1983
- 500 MHz 1H NMR study of the role of lysines and arginines in the binding of gene‐5 protein to oligoadenylic acidsFEBS Letters, 1981
- Studies on DNA UnwindingEuropean Journal of Biochemistry, 1977