1. Crystallization and preliminary X-ray diffraction analysis of brefeldin A-ADP ribosylated substrate (BARS).
- Author
-
Narduni, Marco, Spano, Stefanua, Cericola, Claudia, Pesce, Alessandra, Damonte, Gianluca, Luini, Alberto, Corda, Daniela, and Bolognesia, Martino
- Subjects
ADENOSINE diphosphate ,CRYSTALLIZATION ,ENTEROBACTERIACEAE ,ESCHERICHIA coli ,GRAM-negative bacteria ,PARTICLES (Nuclear physics) - Abstract
Brefeldin A-ADP ribosylated substrate (BARS) is a newly discovered enzyme involved in membrane fission, catalyzing the formation of phosphatidic acid by transfer of an acyl group from acyl-CoA to lysophosphatidic acid. A truncated form of BARS, lacking the C-terminal segment expected to interact with the Golgi membrane, has been expressed in soluble form in Escherichia coli, purified and crystallized. BARS crystals diffract up to 2.5 Å resolution using synchrotron radiation and belong to space group P6
2 22/P64 22, with unit-cell parameters a = b = 89.2, c = 162.6 A, α = β = 90, γ = 120° and one molecule (39.5 kDa) per asymmetric unit. SeMet-substituted BARS has been crystallized under growth conditions very similar to those of the native protein. [ABSTRACT FROM AUTHOR]- Published
- 2002
- Full Text
- View/download PDF