1DXF

2-dehydro-3-deoxy-galactarate aldolase from Escherichia coli in complex with pyruvate

Summary for 1DXF

• Entry DOI: 10.2210/pdb1dxf/pdb
• Related: 1DXE
• Descriptor: 2-DEHYDRO-3-DEOXY-GALACTARATE ALDOLASE, PYRUVIC ACID, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: class ii aldolase
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 2
• Total formula weight: 55234.46

Authors

Izard, T.,Blackwell, N.C. (deposition date: 2000-01-05, release date: 2000-08-25, Last modification date: 2024-11-20)

Primary citation

Izard, T.,Blackwell, N.C.
Crystal Structures of the Metal-Dependent 2-Dehydro-3-Deoxy-Galactarate Aldolase Suggest a Novel Reaction Mechanism.
Embo J., 19:3849-, 2000

PubMed 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.

PubMed: 10921867
DOI: 10.1093/EMBOJ/19.15.3849

Experimental method

X-RAY DIFFRACTION (2.6 Å)