Abstract
A chemical modification of the gene 5 DNA binding protein (G5BP) from bacteriophage fd was investigated using X-ray diffraction and difference Fourier analysis. The crystalline protein was reacted with pentaammineruthenium (III) trichloride, Ru(NH3)5Cl3, a reagent believed specific for histidine residues and useful in NMR and chemical modification studies of proteins. The major ruthenium site was found by difference Fourier analysis to be 4 Å from histidine 64, the only histidine residue in the molecule. A second bipartite site, believed to be a ruthenium-anion pair, appeared to be salt-bridged to glutamic acid 40 and arginine 16. Indications were present in the difference Fourier results to suggest that the β loop containing tyrosine 41 had undergone a slight conformational rearrangement to accommodate this interaction.
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Axelrod, H., DeLozier, G., Greene, S. et al. Modification of the gene 5 DNA unwinding protein with ruthenium. J Protein Chem 4, 235–243 (1985). https://doi.org/10.1007/BF01025301
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DOI: https://doi.org/10.1007/BF01025301