The structure of the gene 5 DNA unwinding protein from bacteriophage fd has been solved to 2.3Å resolution by X-ray diffraction techniques. The molecule contains an extensive cleft region that we have identified as the DNA binding site on the basis of the residues that comprise its surface. The interior of the groove has a rather large number of basic amino acid residues that serve to draw the polynucleotide backbone into the cleft. Arrayed along the external edges of the groove are a number of aromatic amino acid side groups that are in position to stack upon the bases of the DNA and fit it in place. The structure and binding mechanism as we visualize it appear to be fully consistent with evidence provided by physical-chemical studies of the protein in solution.
|Number of pages||9|
|Journal||Journal of Supramolecular and Cellular Biochemistry|
|Publication status||Published - 1979|
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