PMID:8836102
| Citation |
Blom, NS, Tétreault, S, Coulombe, R and Sygusch, J (1996) Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase. Nat. Struct. Biol. 3:856-62 |
|---|---|
| Abstract |
The molecular architecture of the Class II E. coli fructose 1,6-bisphosphate aldolase dimer was determined to 1.6 A resolution. The subunit fold corresponds to a singly wound alpha/beta-barrel with an active site located on the beta-barrel carboxyl side of each subunit. In each subunit there are two mutually exclusive zinc metal ion binding sites, 3.2 A 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 acid residues, are structurally dissimilar, and from sequence comparisons appear to be evolutionary distinct. |
| Links | |
| Keywords |
Binding Sites; Escherichia coli/enzymology; Fructose-Bisphosphate Aldolase/chemistry; Fructose-Bisphosphate Aldolase/metabolism; Protein Conformation; Substrate Specificity |
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