Crystallization of truncated hemolysin A from Proteus mirabilis

Luke Bailey, Sean Agger, Luke Peterson, James Thompson, Todd Weaver

Research output: Contribution to journalArticle

1 Scopus citations

Abstract

Proteus species are second only to Escherichia coli as the most common causative agent of Gram-negative bacteria-based urinary-tract infections and many harbor several virulence factors that provide inherent uropathogenicity. One virulence factor stems from a two-partner secretion pathway comprised of hemolysin A and hemolysin B; upon hemolysin B-dependent secretion, hemolysin A becomes activated. This system is distinct from the classic type I secretion pathway exemplified by the hemolysin system within Escherichia coli. In order to describe the mechanism by which hemolysin A is activated for pore formation, an amino-terminal truncated form capable of complementing the non-secreted full-length hemolysin A and thereby restoring hemolytic activity has been constructed, expressed and purified. A room-temperature data set has been collected to 2.5 Å resolution. The crystal belongs to the orthorhombic space group P21212, with unit-cell parameters a = 34.47, b = 58.40, c = 119.74 Å. The asymmetric unit is expected to contain a single monomer, which equates to a Matthews coefficient of 1.72 Å3 Da-1 and a solvent content of 28.3%.

Original languageEnglish (US)
Pages (from-to)448-450
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume61
Issue number4
DOIs
StatePublished - 2005

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ASJC Scopus subject areas

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

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