Crystallization and preliminary X-ray diffraction analysis of brefeldin A-ADP ribosylated substrate (BARS)

Marco Nardini, Stefania Spanò, Claudia Cericola, Alessandra Pesce, Gianluca Damonte, Alberto Luini, Daniela Corda, Martino Bolognesi

Research output: Contribution to journalArticle

12 Citations (Scopus)

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 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.
Original languageEnglish
Pages (from-to)1068-70
Number of pages3
JournalActa crystallographica. Section D, Biological crystallography
Volume58
Issue numberPt 6 Pt 2
Publication statusPublished - Jun 2002

    Fingerprint

Keywords

  • Animals
  • Carrier Proteins
  • Crystallization
  • Crystallography, X-Ray
  • Protein Conformation
  • Rats
  • Recombinant Proteins
  • Transcription Factors

Cite this

Nardini, M., Spanò, S., Cericola, C., Pesce, A., Damonte, G., Luini, A., ... Bolognesi, M. (2002). Crystallization and preliminary X-ray diffraction analysis of brefeldin A-ADP ribosylated substrate (BARS). Acta crystallographica. Section D, Biological crystallography, 58(Pt 6 Pt 2), 1068-70.