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The adhesive PitA pilus protein from the early dental plaque colonizer Streptococcus oralis: expression, purification, crystallization and X-ray diffraction analysis
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| Zeitschriftentitel: | Acta Crystallographica Section F Structural Biology Communications |
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| Personen und Körperschaften: | , |
| In: | Acta Crystallographica Section F Structural Biology Communications, 76, 2020, 1, S. 8-13 |
| Format: | E-Article |
| Sprache: | Unbestimmt |
| veröffentlicht: |
International Union of Crystallography (IUCr)
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| Schlagwörter: |
| author_facet |
Kumari Yadav, Rajnesh Krishnan, Vengadesan Kumari Yadav, Rajnesh Krishnan, Vengadesan |
|---|---|
| author |
Kumari Yadav, Rajnesh Krishnan, Vengadesan |
| spellingShingle |
Kumari Yadav, Rajnesh Krishnan, Vengadesan Acta Crystallographica Section F Structural Biology Communications The adhesive PitA pilus protein from the early dental plaque colonizer Streptococcus oralis: expression, purification, crystallization and X-ray diffraction analysis Condensed Matter Physics Genetics Biochemistry Structural Biology Biophysics |
| author_sort |
kumari yadav, rajnesh |
| spelling |
Kumari Yadav, Rajnesh Krishnan, Vengadesan 2053-230X International Union of Crystallography (IUCr) Condensed Matter Physics Genetics Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1107/s2053230x1901642x <jats:p>PitA is the putative tip adhesin of the pilus islet 2 (PI-2)-encoded sortase-dependent pilus in the Gram-positive <jats:italic>Streptococcus oralis</jats:italic>, an opportunistic pathogen that often flourishes within the diseased human oral cavity. Early colonization by <jats:italic>S. oralis</jats:italic> and its interaction with <jats:italic>Actinomyces oris</jats:italic> seeds the development of oral biofilm or dental plaque. Here, the PI-2 pilus plays a vital role in mediating adherence to host surfaces and other bacteria. A recombinant form of the PitA adhesin has now been produced and crystallized. Owing to the large size (∼100 kDa), flexibility and complicated folding of PitA, obtaining diffraction-quality crystals has been a challenge. However, by the use of limited proteolysis with α-chymotrypsin, the diffraction quality of the PitA crystals was considerably enhanced to 2.16 Å resolution. These crystals belonged to space group <jats:italic>P</jats:italic>1, with unit-cell parameters <jats:italic>a</jats:italic> = 61.48, <jats:italic>b</jats:italic> = 70.87, <jats:italic>c</jats:italic> = 82.46 Å, α = 80.08, β = 87.02, γ = 87.70°. The anomalous signal from the terbium derivative of α-chymotrypsin-treated PitA crystals prepared with terbium crystallophore (Tb-Xo4) was sufficient to obtain an interpretable electron-density map via terbium SAD phasing.</jats:p> The adhesive PitA pilus protein from the early dental plaque colonizer <i>Streptococcus oralis</i>: expression, purification, crystallization and X-ray diffraction analysis Acta Crystallographica Section F Structural Biology Communications |
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| title |
The adhesive PitA pilus protein from the early dental plaque colonizer Streptococcus oralis: expression, purification, crystallization and X-ray diffraction analysis |
| title_unstemmed |
The adhesive PitA pilus protein from the early dental plaque colonizer Streptococcus oralis: expression, purification, crystallization and X-ray diffraction analysis |
| title_full |
The adhesive PitA pilus protein from the early dental plaque colonizer Streptococcus oralis: expression, purification, crystallization and X-ray diffraction analysis |
| title_fullStr |
The adhesive PitA pilus protein from the early dental plaque colonizer Streptococcus oralis: expression, purification, crystallization and X-ray diffraction analysis |
| title_full_unstemmed |
The adhesive PitA pilus protein from the early dental plaque colonizer Streptococcus oralis: expression, purification, crystallization and X-ray diffraction analysis |
| title_short |
The adhesive PitA pilus protein from the early dental plaque colonizer Streptococcus oralis: expression, purification, crystallization and X-ray diffraction analysis |
| title_sort |
the adhesive pita pilus protein from the early dental plaque colonizer <i>streptococcus oralis</i>: expression, purification, crystallization and x-ray diffraction analysis |
| topic |
Condensed Matter Physics Genetics Biochemistry Structural Biology Biophysics |
| url |
http://dx.doi.org/10.1107/s2053230x1901642x |
| publishDate |
2020 |
| physical |
8-13 |
| description |
<jats:p>PitA is the putative tip adhesin of the pilus islet 2 (PI-2)-encoded sortase-dependent pilus in the Gram-positive <jats:italic>Streptococcus oralis</jats:italic>, an opportunistic pathogen that often flourishes within the diseased human oral cavity. Early colonization by <jats:italic>S. oralis</jats:italic> and its interaction with <jats:italic>Actinomyces oris</jats:italic> seeds the development of oral biofilm or dental plaque. Here, the PI-2 pilus plays a vital role in mediating adherence to host surfaces and other bacteria. A recombinant form of the PitA adhesin has now been produced and crystallized. Owing to the large size (∼100 kDa), flexibility and complicated folding of PitA, obtaining diffraction-quality crystals has been a challenge. However, by the use of limited proteolysis with α-chymotrypsin, the diffraction quality of the PitA crystals was considerably enhanced to 2.16 Å resolution. These crystals belonged to space group <jats:italic>P</jats:italic>1, with unit-cell parameters <jats:italic>a</jats:italic> = 61.48, <jats:italic>b</jats:italic> = 70.87, <jats:italic>c</jats:italic> = 82.46 Å, α = 80.08, β = 87.02, γ = 87.70°. The anomalous signal from the terbium derivative of α-chymotrypsin-treated PitA crystals prepared with terbium crystallophore (Tb-Xo4) was sufficient to obtain an interpretable electron-density map via terbium SAD phasing.</jats:p> |
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| description | <jats:p>PitA is the putative tip adhesin of the pilus islet 2 (PI-2)-encoded sortase-dependent pilus in the Gram-positive <jats:italic>Streptococcus oralis</jats:italic>, an opportunistic pathogen that often flourishes within the diseased human oral cavity. Early colonization by <jats:italic>S. oralis</jats:italic> and its interaction with <jats:italic>Actinomyces oris</jats:italic> seeds the development of oral biofilm or dental plaque. Here, the PI-2 pilus plays a vital role in mediating adherence to host surfaces and other bacteria. A recombinant form of the PitA adhesin has now been produced and crystallized. Owing to the large size (∼100 kDa), flexibility and complicated folding of PitA, obtaining diffraction-quality crystals has been a challenge. However, by the use of limited proteolysis with α-chymotrypsin, the diffraction quality of the PitA crystals was considerably enhanced to 2.16 Å resolution. These crystals belonged to space group <jats:italic>P</jats:italic>1, with unit-cell parameters <jats:italic>a</jats:italic> = 61.48, <jats:italic>b</jats:italic> = 70.87, <jats:italic>c</jats:italic> = 82.46 Å, α = 80.08, β = 87.02, γ = 87.70°. The anomalous signal from the terbium derivative of α-chymotrypsin-treated PitA crystals prepared with terbium crystallophore (Tb-Xo4) was sufficient to obtain an interpretable electron-density map via terbium SAD phasing.</jats:p> |
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| spelling | Kumari Yadav, Rajnesh Krishnan, Vengadesan 2053-230X International Union of Crystallography (IUCr) Condensed Matter Physics Genetics Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1107/s2053230x1901642x <jats:p>PitA is the putative tip adhesin of the pilus islet 2 (PI-2)-encoded sortase-dependent pilus in the Gram-positive <jats:italic>Streptococcus oralis</jats:italic>, an opportunistic pathogen that often flourishes within the diseased human oral cavity. Early colonization by <jats:italic>S. oralis</jats:italic> and its interaction with <jats:italic>Actinomyces oris</jats:italic> seeds the development of oral biofilm or dental plaque. Here, the PI-2 pilus plays a vital role in mediating adherence to host surfaces and other bacteria. A recombinant form of the PitA adhesin has now been produced and crystallized. Owing to the large size (∼100 kDa), flexibility and complicated folding of PitA, obtaining diffraction-quality crystals has been a challenge. However, by the use of limited proteolysis with α-chymotrypsin, the diffraction quality of the PitA crystals was considerably enhanced to 2.16 Å resolution. These crystals belonged to space group <jats:italic>P</jats:italic>1, with unit-cell parameters <jats:italic>a</jats:italic> = 61.48, <jats:italic>b</jats:italic> = 70.87, <jats:italic>c</jats:italic> = 82.46 Å, α = 80.08, β = 87.02, γ = 87.70°. The anomalous signal from the terbium derivative of α-chymotrypsin-treated PitA crystals prepared with terbium crystallophore (Tb-Xo4) was sufficient to obtain an interpretable electron-density map via terbium SAD phasing.</jats:p> The adhesive PitA pilus protein from the early dental plaque colonizer <i>Streptococcus oralis</i>: expression, purification, crystallization and X-ray diffraction analysis Acta Crystallographica Section F Structural Biology Communications |
| spellingShingle | Kumari Yadav, Rajnesh, Krishnan, Vengadesan, Acta Crystallographica Section F Structural Biology Communications, The adhesive PitA pilus protein from the early dental plaque colonizer Streptococcus oralis: expression, purification, crystallization and X-ray diffraction analysis, Condensed Matter Physics, Genetics, Biochemistry, Structural Biology, Biophysics |
| title | The adhesive PitA pilus protein from the early dental plaque colonizer Streptococcus oralis: expression, purification, crystallization and X-ray diffraction analysis |
| title_full | The adhesive PitA pilus protein from the early dental plaque colonizer Streptococcus oralis: expression, purification, crystallization and X-ray diffraction analysis |
| title_fullStr | The adhesive PitA pilus protein from the early dental plaque colonizer Streptococcus oralis: expression, purification, crystallization and X-ray diffraction analysis |
| title_full_unstemmed | The adhesive PitA pilus protein from the early dental plaque colonizer Streptococcus oralis: expression, purification, crystallization and X-ray diffraction analysis |
| title_short | The adhesive PitA pilus protein from the early dental plaque colonizer Streptococcus oralis: expression, purification, crystallization and X-ray diffraction analysis |
| title_sort | the adhesive pita pilus protein from the early dental plaque colonizer <i>streptococcus oralis</i>: expression, purification, crystallization and x-ray diffraction analysis |
| title_unstemmed | The adhesive PitA pilus protein from the early dental plaque colonizer Streptococcus oralis: expression, purification, crystallization and X-ray diffraction analysis |
| topic | Condensed Matter Physics, Genetics, Biochemistry, Structural Biology, Biophysics |
| url | http://dx.doi.org/10.1107/s2053230x1901642x |