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

Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):1068-70. doi: 10.1107/s0907444902006984. Epub 2002 May 29.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carrier Proteins / chemistry*
  • Carrier Proteins / isolation & purification
  • Crystallization
  • Crystallography, X-Ray
  • Protein Conformation
  • Rats
  • Recombinant Proteins / chemistry
  • Transcription Factors*

Substances

  • Carrier Proteins
  • Ctbp1 protein, rat
  • Recombinant Proteins
  • Transcription Factors