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Purification, crystallization and data collection of methicillin-resistant Staphylococcus aureus Sar2676, a pantothenate synthetase

  • Jaldappagari Seetharamappa
  • , Muse Oke
  • , Huanting Liu
  • , Stephen A. McMahon
  • , Kenneth A. Johnson
  • , Lester Carter
  • , Mark Dorward
  • , Michal Zawadzki
  • , Ian M. Overton
  • , C. A.Johannes Van Niekirk
  • , Shirley Graham
  • , Catherine H. Botting
  • , Garry L. Taylor
  • , Malcolm F. White
  • , Geoffrey J. Barton
  • , Peter J. Coote
  • , James H. Naismith

Research output: Contribution to journalArticlepeer-review

Abstract

Sar2676, a pantothenate synthetase with a molecular weight of 31 419 Da from methicillin-resistant Staphylococcus aureus, has been expressed, purified and crystallized at 293 K. The protein crystallizes in a primitive triclinic lattice, with unit-cell parameters a = 45.3, b = 60.5, c = 117.6 Å, α = 87.2, β = 81.2, γ = 68.4°. A complete data set has been collected to 2.3 Å resolution at the ESRF. Consideration of the likely solvent content suggested the asymmetric unit to contain four molecules. This has been confirmed by molecular-replacement phasing calculations, which give a solution with four monomers using a monomer of pantothenate synthetase from Escherichia coli (PDB code 1iho), which is 41% identical to Sar2676, as a search model.

Original languageEnglish
Pages (from-to)488-491
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume63
Issue number6
DOIs
Publication statusPublished - 5 May 2007

Keywords

  • Methicillin-resistant Staphylococcus aureus
  • Pantothenate synthetase
  • Sar2676

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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