1dxe | pdb_00001dxe
2-DEHYDRO-3-DEOXY-GALACTARATE ALDOLASE FROM ESCHERICHIA COLI
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| 1dxe, resolution 1.8Å | |||||||||||||
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| Ligands: | PO4 and MG | ||||||||||||
| Activity: | 2-dehydro-3-deoxyglucarate aldolase, with EC number 4.1.2.20 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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.
About this Structure
1DXE is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structures of the metal-dependent 2-dehydro-3-deoxy-galactarate aldolase suggest a novel reaction mechanism., Izard T, Blackwell NC, EMBO J. 2000 Aug 1;19(15):3849-56. PMID:10921867
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