Crystallization and preliminary X-ray diffraction analysis of YisP protein from Bacillus subtilis subsp. subtilis strain 168

Yumei Hu, Shiru Jia, Feifei Ren, Chun Hsiang Huang, Tzu Ping Ko, Douglas A. Mitchell, Rey Ting Guo, Yingying Zheng

Research output: Contribution to journalArticlepeer-review

Abstract

YisP is an enzyme involved in the pathway of biofilm formation in bacteria and is predicted to possess squalene synthase activity. A BlastP search using the YisP protein sequence from Bacillus subtilis subsp. subtilis strain 168 shows that it shares 23% identity with the dehydrosqualene synthase from Staphylococcus aureus. The YisP from B. subtilis 168 was expressed in Escherichia coli and the recombinant protein was purified and crystallized. The crystals, which belong to the orthorhombic space group P212121, with unit-cell parameters a = 43.966, b = 77.576, c = 91.378 Å, were obtained by the sitting-drop vapour-diffusion method and diffracted to 1.92 Å resolution. Structure determination using MAD and MIR methods is in progress.

Original languageEnglish (US)
Pages (from-to)77-79
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume69
Issue number1
DOIs
StatePublished - Jan 2013

Keywords

  • Bacillus subtilis subsp. subtilis
  • YisP
  • dehydrosqualene synthase
  • drug design
  • squalene synthase
  • synchrotron radiation

ASJC Scopus subject areas

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

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