Crystallization of dienelactone hydrolase in two space groups: structural changes caused by crystal packing

Acta Crystallogr F Struct Biol Commun. 2014 Jul;70(Pt 7):884-9. doi: 10.1107/S2053230X1401108X. Epub 2014 Jun 18.


Dienelactone hydrolase (DLH) is a monomeric protein with a simple α/β-hydrolase fold structure. It readily crystallizes in space group P2₁2₁2₁ from either a phosphate or ammonium sulfate precipitation buffer. Here, the structure of DLH at 1.85 Å resolution crystallized in space group C2 with two molecules in the asymmetric unit is reported. When crystallized in space group P2₁2₁2₁ DLH has either phosphates or sulfates bound to the protein in crucial locations, one of which is located in the active site, preventing substrate/inhibitor binding. Another is located on the surface of the enzyme coordinated by side chains from two different molecules. Crystallization in space group C2 from a sodium citrate buffer results in new crystallographic protein-protein interfaces. The protein backbone is highly similar, but new crystal contacts cause changes in side-chain orientations and in loop positioning. In regions not involved in crystal contacts, there is little change in backbone or side-chain configuration. The flexibility of surface loops and the adaptability of side chains are important factors enabling DLH to adapt and form different crystal lattices.

Keywords: crystal packing; dienelactone hydrolase.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Carboxylic Ester Hydrolases / chemistry*
  • Carboxylic Ester Hydrolases / genetics
  • Carboxylic Ester Hydrolases / metabolism
  • Citrates / chemistry
  • Crystallography, X-Ray
  • Models, Molecular
  • Phosphates / chemistry
  • Protein Folding
  • Protein Interaction Domains and Motifs
  • Protein Structure, Secondary
  • Pseudomonas / chemistry*
  • Pseudomonas / enzymology
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Sodium Citrate
  • Sulfates / chemistry


  • Bacterial Proteins
  • Citrates
  • Phosphates
  • Recombinant Proteins
  • Sulfates
  • Sodium Citrate
  • Carboxylic Ester Hydrolases
  • carboxymethylenebutenolidase

Associated data

  • PDB/4P92
  • PDB/4P93