Crystallization and preliminary X-ray analysis of the C-terminal fragment of PorM, a subunit of the Porphyromonas gingivalis type IX secretion system

Acta Crystallogr F Struct Biol Commun. 2015 Jan 1;71(Pt 1):71-4. doi: 10.1107/S2053230X1402559X. Epub 2015 Jan 1.

Abstract

PorM is a membrane protein involved in the assembly of the type IX secretion system (T9SS) from Porphyromonas gingivalis, a major bacterial pathogen responsible for periodontal disease in humans. The periplasmic domain of PorM was overexpressed in Escherichia coli and purified. A fragment of the purified protein was obtained by limited proteolysis. Crystals of this fragment belonged to the tetragonal space group P4(3)2(1)2. Native and MAD data sets were recorded to 2.85 and 3.1 Å resolution, respectively, using synchrotron radiation.

Keywords: Porphyromonas gingivalis; T9SS.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / isolation & purification
  • Bacterial Secretion Systems
  • Chromatography, Gel
  • Crystallization
  • Crystallography, X-Ray
  • Porphyromonas gingivalis*
  • Protein Structure, Tertiary
  • Protein Subunits

Substances

  • Bacterial Proteins
  • Bacterial Secretion Systems
  • Protein Subunits