Abstract
Capsular polysaccharides (CPs) are important virulence factors of Staphylococcus aureus. The biosynthesis of type 5 and type 8 CPs (CP5 and CP8), which are produced by most clinical isolates of S. aureus, is catalyzed by 16 CP-assembling proteins. One of these proteins is the enzyme CapF, which catalyzes the synthesis of UDP-N-acetyl-l-fucosamine, a component of both CP5 and CP8. Here, the cloning, expression, purification, crystallization and diffraction analysis of CapF are reported. Optimization of the crystallization conditions by differential scanning calorimetry afforded a crystal of selenomethionine-substituted CapF that diffracted to a resolution of 2.80 Å. The crystal belongs to space group P3221, with unit-cell parameters a = b = 119.6, c = 129.5 Å.
Original language | English |
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Pages (from-to) | 512-515 |
Number of pages | 4 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 64 |
Issue number | 6 |
DOIs | |
Publication status | Published - 2008 |
Externally published | Yes |
Keywords
- Capsular polysaccharide-synthesis enzymes
- Differential scanning calorimetry
- Staphylococcus aureus
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics