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JBC, Vol. 250, Issue 19, 7663-7667, Oct, 1975

Metal ion binding in triclinic lysozyme

K. Kurachi, L. C. Sieker and L. H. Jensen

The binding sites of Mn2+, Co2+, and Gd3+ have been determined in triclinic lysozyme at pH 4.5 to 4.6. Mn2+ and Co2+ bind a site approximately 2.5 A from 1 of the oxygen atoms of the Glu-35 chain. The occupancy of the Mn2+ site is 0.22, corresponding to 1 bound ion for each 4.6 protein molecules. The occupancy of the Co2+ site is much lower, about 0.048. Gd3+ appears to be bound at two sites, the main one 2.5 A from an oxygen atom of the Glu-35 side chain, the other 3.1 A from an oxygen atom of the Asp-52 chain. The occupancy of both Gd3+ sites is low, 0.036 and 0.016, the latter being so low that the presence of the ion at this site is in doubt. The binding site of Mn2+ in the di(N-acetylglucosamine)-lysozyme complex has also been determined. It does not differ significantly from the Mn2+ binding site in the native protein, but the occupancy is lower, 0.16.
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				A. M. Deacon, C. M. Weeks, R. Miller, and S. E. Ealick The Shake-and-Bake structure determination of triclinic lysozyme PNAS, August 4, 1998; 95(16): 9284 - 9289. [Abstract] [Full Text] [PDF]