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

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Brefeldin A
Crystallization
X-Ray Diffraction
Adenosine Diphosphate
Acyl Coenzyme A
Phosphatidic Acids
Synchrotrons
Membranes
Radiation
Escherichia coli
Enzymes
Growth
Proteins

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.

Crystallization and preliminary X-ray diffraction analysis of brefeldin A-ADP ribosylated substrate (BARS). / Nardini, Marco; Spanò, Stefania; Cericola, Claudia; Pesce, Alessandra; Damonte, Gianluca; Luini, Alberto; Corda, Daniela; Bolognesi, Martino.

In: Acta crystallographica. Section D, Biological crystallography, Vol. 58, No. Pt 6 Pt 2, 06.2002, p. 1068-70.

Research output: Contribution to journalArticle

Nardini, M, Spanò, S, Cericola, C, Pesce, A, Damonte, G, Luini, A, Corda, D & Bolognesi, M 2002, 'Crystallization and preliminary X-ray diffraction analysis of brefeldin A-ADP ribosylated substrate (BARS)', Acta crystallographica. Section D, Biological crystallography, vol. 58, no. Pt 6 Pt 2, pp. 1068-70.
Nardini, Marco ; Spanò, Stefania ; Cericola, Claudia ; Pesce, Alessandra ; Damonte, Gianluca ; Luini, Alberto ; Corda, Daniela ; Bolognesi, Martino. / Crystallization and preliminary X-ray diffraction analysis of brefeldin A-ADP ribosylated substrate (BARS). In: Acta crystallographica. Section D, Biological crystallography. 2002 ; Vol. 58, No. Pt 6 Pt 2. pp. 1068-70.
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T1 - Crystallization and preliminary X-ray diffraction analysis of brefeldin A-ADP ribosylated substrate (BARS)

AU - Nardini, Marco

AU - Spanò, Stefania

AU - Cericola, Claudia

AU - Pesce, Alessandra

AU - Damonte, Gianluca

AU - Luini, Alberto

AU - Corda, Daniela

AU - Bolognesi, Martino

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AB - 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.

KW - Animals

KW - Carrier Proteins

KW - Crystallization

KW - Crystallography, X-Ray

KW - Protein Conformation

KW - Rats

KW - Recombinant Proteins

KW - Transcription Factors

M3 - Article

VL - 58

SP - 1068

EP - 1070

JO - Acta crystallographica. Section D, Biological crystallography

JF - Acta crystallographica. Section D, Biological crystallography

SN - 0907-4449

IS - Pt 6 Pt 2

ER -