Fructose-1,6-bisphosphate aldolase, crystal

Cooper, S. J., Leonard, G. A., McSweeney, S. M., Thompson, A. W., Naismith, J. H., Qamar, S., et al. The Crystal Structure of a Class II Fructose-1,6-Bisphosphate Aldolase Shows a Novel Binuclear Metal-Binding Active Site Embedded in a Familiar Fold. Structure 1996, 4, 1303-1315. 

Hall, D. R., Leonard, G. A., Reed, C. D., Watt, C. I., Berry, A., Hunter, W. N. The Crystal Structure of Escherichia coli Class II Fructose-1,6-Bisphosphate Aldolase in Complex with Phosphoglycolohydroxamate Reveals Details of Mechanism and Specificity. J. Mol. Biol. 1999, 287, 383-394. 

S. J. Cooper, G.A. Leonard, S.M. McSweeney, A.W. Thompson, J.H. Naismith, S. Qamar, A. Plater, A. Berry, and W.N. Hunter. 1996. The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel hinuclear metalbinding active site embedded in a familiar fold Structure 4 1303-1315. (PubMed)... 

For class I type enzymes, the (/ia)8-barrel structure of the class I fructose 1,6-bisphosphate aldolase (FruA, vide infra) from rabbit muscle was the first to be uncovered by X-ray crystal-structure analysis [33] this was followed by those from several other species [34-37]. A complex of the aldolase with non-covalently bound substrate DHAP (dihydroxyacetone phosphate) in the active site indicates a trajectory for the substrate traveling towards the nucleophilic Lys229 N [38, 39]. There, the proximity of side-chains Lysl46 and Glul87 is consistent with their participation as proton donors and acceptors in Schiff base formation (A, B) this was further supported by site-directed mutagenesis studies [40]. 

Dalby, A., Dauter, Z., and Littlechild, J. A., Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate Mechanistic implications. Protein Sci. 1999, 8 (2), 291-297. 

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