Abstract
| Original language | Unknown |
|---|---|
| Pages (from-to) | 269-271 |
| Journal | Acta Crystallographica Section F-Structural Biology And Crystallization Com |
| Volume | 66 |
| Issue number | Part 3 |
| DOIs | |
| Publication status | Published - 1 Jan 2010 |
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Cloning, expression, purification, crystallization and preliminary crystallographic studies of BceC, a UDP-glucose dehydrogenase from Burkholderia cepacia IST408. / Frazao, Carlos Maria.
In: Acta Crystallographica Section F-Structural Biology And Crystallization Com, Vol. 66, No. Part 3, 01.01.2010, p. 269-271.Research output: Contribution to journal › Article
TY - JOUR
T1 - Cloning, expression, purification, crystallization and preliminary crystallographic studies of BceC, a UDP-glucose dehydrogenase from Burkholderia cepacia IST408
AU - Frazao, Carlos Maria
PY - 2010/1/1
Y1 - 2010/1/1
N2 - Bacteria of the Burkholderia cepacia complex (Bcc) have emerged as important opportunistic pathogens, establishing lung infections in immunocompromised or cystic fibrosis patients. Bcc uses polysaccharide-biofilm production in order to evade the host immune response. The biofilm precursor UDP-glucuronic acid is produced by a twofold NAD(+)-dependent oxidation of UDP-glucose. In B. cepacia IST408 this enzymatic reaction is performed by the UDP-glucose dehydrogenase BceC, a 470-residue enzyme, the production and crystallization of which are described here. The crystals belonged to the orthorhombic space group P2(1)2(1)2(1) and contained four molecules in the asymmetric unit. Their crystallographic analysis at 2.09 angstrom resolution and a molecular-replacement study are reported.
AB - Bacteria of the Burkholderia cepacia complex (Bcc) have emerged as important opportunistic pathogens, establishing lung infections in immunocompromised or cystic fibrosis patients. Bcc uses polysaccharide-biofilm production in order to evade the host immune response. The biofilm precursor UDP-glucuronic acid is produced by a twofold NAD(+)-dependent oxidation of UDP-glucose. In B. cepacia IST408 this enzymatic reaction is performed by the UDP-glucose dehydrogenase BceC, a 470-residue enzyme, the production and crystallization of which are described here. The crystals belonged to the orthorhombic space group P2(1)2(1)2(1) and contained four molecules in the asymmetric unit. Their crystallographic analysis at 2.09 angstrom resolution and a molecular-replacement study are reported.
KW - EXOPOLYSACCHARIDE
KW - COMPLEX
KW - CRYSTALS
U2 - 10.1107/s1744309109053500
DO - 10.1107/s1744309109053500
M3 - Article
VL - 66
SP - 269
EP - 271
JO - Acta Crystallographica Section F-Structural Biology And Crystallization Com
JF - Acta Crystallographica Section F-Structural Biology And Crystallization Com
SN - 1744-3091
IS - Part 3
ER -