Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase

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Abstract
The molecular architecture of the Class II E. coli fructose 1,6-bisphosphate aldolase dimer was determined to 1.6 Angstrom resolution. The subunit fold corresponds to a singly wound alpha/beta-barrel with an active site located on the beta-barret carboxyl side of each subunit. In each subunit there are two mutually exclusive zinc metal ion binding sites, 3.2 Angstrom apart; the exclusivity is mediated by a conformational transition involving side-chain rotations by chelating histidine residues. A binding site for K+ and NH4+ activators was found near the beta-barrel centre. Although Class I and Class II aldolases catalyse identical reactions, their active sites do not share common amino add residues, are structurally dissimilar, and from sequence comparisons appear to be evolutionary distinct.