PMID:10921867

Citation	Izard, T and Blackwell, NC (2000) Crystal structures of the metal-dependent 2-dehydro-3-deoxy-galactarate aldolase suggest a novel reaction mechanism. EMBO J. 19:3849-56
Abstract	Carbon-carbon bond formation is an essential reaction in organic chemistry and the use of aldolase enzymes for the stereochemical control of such reactions is an attractive alternative to conventional chemical methods. Here we describe the crystal structures of a novel class II enzyme, 2-dehydro-3-deoxy-galactarate (DDG) aldolase from Escherichia coli, in the presence and absence of substrate. The crystal structure was determined by locating only four Se sites to obtain phases for 506 protein residues. The protomer displays a modified (alpha/beta)(8) barrel fold, in which the eighth alpha-helix points away from the beta-barrel instead of packing against it. Analysis of the DDG aldolase crystal structures suggests a novel aldolase mechanism in which a phosphate anion accepts the proton from the methyl group of pyruvate.
Links	PubMed PMC306599 Online version:10.1093/emboj/19.15.3849
Keywords	Aldehyde-Lyases/chemistry; Aldehyde-Lyases/classification; Crystallography, X-Ray; Escherichia coli/enzymology; Models, Molecular; Protein Structure, Secondary; Protein Structure, Tertiary; Pyruvic Acid/metabolism; Selenomethionine/chemistry; Sugar Acids/metabolism; Tartronates
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