PMID:12595741

Citation	Hall, DR, Kemp, LE, Leonard, GA, Marshall, K, Berry, A and Hunter, WN (2003) The organization of divalent cations in the active site of cadmium Escherichia coli fructose-1,6-bisphosphate aldolase. Acta Crystallogr. D Biol. Crystallogr. 59:611-4
Abstract	Previously determined crystal structures of the zinc enzyme Escherichia coli class II fructose-1,6-bisphosphate aldolase display good agreement for the protein structure but a differing metal-ion organization in the active site. The structure of the enzyme with Cd(2+) in place of Zn(2+) has now been determined to 2.0 A resolution to facilitate cation identification. The protein structure was essentially identical to other structures and five Cd(2+) positions were identified. Two of the cations are at the active site; one corresponds to the catalytic ion and the other provides a structural contribution. These Cd(2+) sites are equivalent to two Zn(2+) ions observed when the enzyme is complexed with a transition-state mimic and confirm our assignment of the roles played by these ions.
Links	PubMed
Keywords	Binding Sites; Cadmium/chemistry; Catalysis; Cations/chemistry; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Fructose-Bisphosphate Aldolase/chemistry; Fructose-Bisphosphate Aldolase/isolation & purification; Models, Molecular; Zinc/chemistry
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