A model for the complex between the helix destabilizing protein GP32 of bacteriophage T4 and single-stranded DNA.
A model for the structure of the complex between the helix-destabilizing protein of bacteriophage T4, GP32, and single-stranded DNA is proposed. In this model the bases are arranged in a helix, that is characterized by a relatively large distance between successive bases, a substantial base tilt, in combination with a small rotation per base. This helix is further organized into a tertiary structure, possibly a superhelix, of which the corresponding protein shell corresponds to the relatively rigid and rod-like structure that is observed in hydrodynamic experiments. It is proposed that similar structural features apply to other single-stranded DNA binding proteins in complex with polynucleotides.
Scheerhagen
M A
MA
Department of Biophysics, Free University Amsterdam, The Netherlands.
Kuil
M E
ME
van Amerongen
H
H
van Grondelle
R
R
D004265:DNA Helicases; D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins; D008958:Models, Molecular; D011487:Protein Conformation; D013604:T-Phages / Q000235:genetics*; D014764:Viral Proteins
D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins; D014764:Viral Proteins; C060035:gp32 protein, Enterobacteria phage T4; C027729:helix-destabilizing proteins; D004265:DNA Helicases