The crystal structure of dihydrodipicolinate synthase from Escherichia coli with bound pyruvate and succinic acid semialdehyde: unambiguous resolution of the stereochemistry of the condensation product

Proteins. 2012 Aug;80(8):2117-22. doi: 10.1002/prot.24106. Epub 2012 Jun 4.


The crystal structure of Escherichia coli dihydrodipicolinate synthase with pyruvate and substrate analogue succinic acid semialdehyde condensed with the active site lysine-161 was solved to a resolution of 2.3 Å. Comparative analysis to a previously reported structure both resolves the configuration at the aldol addition center, where the final addition product clearly displays the (S)-configuration, and the final conformation of the adduct within the active site. Direct comparison to two other crystal structures found in the Protein Data Bank, 1YXC, and 3DU0, demonstrates significant similarity between the active site residues of these structures.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Binding Sites
  • Catalytic Domain
  • Crystallography, X-Ray*
  • Escherichia coli*
  • Hydro-Lyases / chemistry*
  • Ligands
  • Protein Conformation*
  • Protein Multimerization
  • Pyruvic Acid / chemistry
  • gamma-Aminobutyric Acid / analogs & derivatives
  • gamma-Aminobutyric Acid / chemistry


  • Ligands
  • gamma-Aminobutyric Acid
  • Pyruvic Acid
  • Hydro-Lyases
  • 4-hydroxy-tetrahydrodipicolinate synthase
  • succinic semialdehyde