PMID:15233803

Citation	Zimenkov, YV, Salminen, A, Efimova, IS, Lahti, R and Baykov, AA (2004) Cd(2+)-induced aggregation of Escherichia coli pyrophosphatase. Eur. J. Biochem. 271:3064-7
Abstract	We report here that Escherichia coli pyrophosphatase aggregates in the presence of millimolar Cd(2+). This highly cooperative process was specific to both the metal ion and the protein and could be reversed fully by decreasing the Cd(2+) concentration. Aggregation was enhanced by Mg(2+), the natural cofactor of pyrophosphatase, and Mn(2+). Mutations at the intersubunit metal-binding site had no effect, whereas mutation at Glu139, which is part of the peripheral metal-binding site found in pyrophosphatase crystals near the contact region between two enzyme molecules, suppressed aggregation. These findings indicate that aggregation is affected by Cd(2+) binding to the peripheral metal-binding site, probably by strengthening intermolecular Trp149-Trp149' stacking interactions.
Links	PubMed Online version:10.1111/j.1432-1033.2004.04239.x
Keywords	Binding Sites; Cadmium/metabolism; Escherichia coli/enzymology; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Magnesium/metabolism; Manganese/metabolism; Models, Molecular; Protein Structure, Secondary; Pyrophosphatases/chemistry; Pyrophosphatases/genetics; Pyrophosphatases/metabolism
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