Topological comparison of two helix destabilizing proteins: ribonuclease A and the gene 5 DNA binding protein.
A topological comparison of the two helix destabilizing proteins, pancreatic ribonuclease A and the gene 5 DNA binding protein of bacteriophage fd has been completed utilizing the available high resolution tertiary structures of each protein. The results indicate these two proteins are structurally if not also evolutionarily related. Regions of closet topological equivalence occur between beta loops directly involved in nucleotide binding or are required for the maintenance of their respective oligonucleotide binding channels. In addition, there is a similar placement of critical amino acid side chains about the binding site. Further evidence for this structural relationship is obtained by comparison of structural data for the mode of complexation of polynucleotides to each protein. The results of topological comparison suggest the essential property shared by helix destabilizing proteins, whether specialized DNA binding proteins such as G5BP or proteins with other primary functional roles, like ribonuclease A, is the presence of an elongated oligonucleotide binding channel. Although ribonuclease A and G5BP are structurally related, it seems likely any protein with this structural feature will exhibit a helix destabilizing capacity. This conclusion is supported by the diversity of molecular characteristics shown by other proteins having this activity.
Brayer
G D
GD
Department of Biochemistry, University of British Columbia, Vancouver, Canada.
McPherson
A
A
D004265:DNA Helicases; D004268:DNA-Binding Proteins; D015394:Molecular Structure; D011487:Protein Conformation; D012259:Ribonuclease, Pancreatic; D014764:Viral Proteins
D004268:DNA-Binding Proteins; D014764:Viral Proteins; C057816:gene 5 protein, Enterobacteria phage M13; C060035:gp32 protein, Enterobacteria phage T4; C027729:helix-destabilizing proteins; D012259:Ribonuclease, Pancreatic; D004265:DNA Helicases