Abstract
The bacteriophage fd gene 5 protein (G5P) binds strongly to single stranded DNA. Electrostatic interactions, involving ion pairing of positively charged lysine and arginine protein side chains with the negatively charged phosphates of four nucleotidyl units of DNA, are very important in this interaction process1–3. However, implication of specific lysyl residues in the DNA-binding site is more difficult. X-ray crystal structure and modeling studies of G5P have been used4,5 to obtain a structural binding model which only includes one (Lys-46) of its six lysyl residues. However, chemical modification studies6 seem to implicate three lysyl residues (Lys-24, 46 and 69) in the nucleic acid binding site of G5P.
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