Crystallization and preliminary X-ray diffraction analysis of brefeldin A-ADP ribosylated substrate (BARS).
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 A resolution using synchrotron radiation and belong to space group P6(2)22/P6(4)22, with unit-cell parameters a = b = 89.2, c = 162.6 A, alpha = beta = 90, gamma = 120 degrees 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.
Nardini
Marco
M
Department of Physics and INFM, University of Genova c/o Advanced Biotechnology Center, Largo Rosanna Benzi 10, 16132 Genova, Italy.
Spanò
Stefania
S
Cericola
Claudia
C
Pesce
Alessandra
A
Damonte
Gianluca
G
Luini
Alberto
A
Corda
Daniela
D
Bolognesi
Martino
M
D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry; D014157:Transcription Factors
D002352:Carrier Proteins; C119945:Ctbp1 protein, rat; D011994:Recombinant Proteins; D014157:Transcription Factors