title: Crystallization of dienelactone hydrolase in two space groups: structural changes caused by crystal packing.
abstract: 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.
authors.affiliation: Research School of Chemistry, Australian National University, Building 137, Sullivans Creek Road, Canberra, ACT 0200, Australia.
authors.forename: Joanne L
authors.initials: JL
authors.lastname: Porter
authors.affiliation: Research School of Chemistry, Australian National University, Building 137, Sullivans Creek Road, Canberra, ACT 0200, Australia.
authors.forename: Paul D
authors.initials: PD
authors.lastname: Carr
authors.affiliation: School of Molecular Bioscience, University of Sydney, Biochemistry Building, Sydney, NSW 2006, Australia.
authors.forename: Charles A
authors.initials: CA
authors.lastname: Collyer
authors.affiliation: Research School of Chemistry, Australian National University, Building 137, Sullivans Creek Road, Canberra, ACT 0200, Australia.
authors.forename: David L
authors.initials: DL
authors.lastname: Ollis
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D002951:Citrates / Q000737:chemistry; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D010710:Phosphates / Q000737:chemistry; D017510:Protein Folding; D054730:Protein Interaction Domains and Motifs; D017433:Protein Structure, Secondary; D011549:Pseudomonas / Q000737:chemistry* / Q000201:enzymology; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D000077559:Sodium Citrate; D013431:Sulfates / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D002951:Citrates; D010710:Phosphates; D011994:Recombinant Proteins; D013431:Sulfates; D000077559:Sodium Citrate; D002265:Carboxylic Ester Hydrolases; C046130:carboxymethylenebutenolidase
keywords: crystal packing; dienelactone hydrolase