4P93

Structure of Dienelactone Hydrolase at 1.85 A resolution crystallised in the C2 space group

Summary for 4P93

• Entry DOI: 10.2210/pdb4p93/pdb
• Related: 4P92
• Descriptor: Carboxymethylenebutenolidase (2 entities in total)
• Functional Keywords: hydrolase, a/b hydrolase fold
• Biological source: Pseudomonas sp.
• Total number of polymer chains: 2
• Total formula weight: 50991.49

Authors

Porter, J.L.,Carr, P.D.,Collyer, C.A.,Ollis, D.L. (deposition date: 2014-04-02, release date: 2014-07-09, Last modification date: 2023-12-20)

Primary citation

Porter, J.L.,Carr, P.D.,Collyer, C.A.,Ollis, D.L.
Crystallization of dienelactone hydrolase in two space groups: structural changes caused by crystal packing.
Acta Crystallogr.,Sect.F, 70:884-889, 2014

PubMed 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.

PubMed: 25005082
DOI: 10.1107/S2053230X1401108X

Experimental method

X-RAY DIFFRACTION (1.85 Å)