Abstract
The Gram negative bacterium Burkholderia pseudomallei is the causative agent of melioidosis. d glycero β d manno Heptose 1 phosphate adenylyltransferase (HldC) is the fourth enzyme of the ADP l glycero β d manno heptose biosynthesis pathway, which produces an essential carbohydrate comprising the inner core of lipopolysaccharide. Therefore, HldC is a potential target of antibiotics against melioidosis. In this study, HldC from B. pseudomallei has been cloned, expressed, purified and crystallized. Synchrotron X ray data from a selenomethionine substituted HldC crystal were also collected to 2.8 Å resolution. The crystal belonged to the primitive triclinic space group P1, with unit cell parameters a = 74.0, b = 74.0, c = 74.9 Å, α = 108.4, β = 108.4, γ = 108.0°. Eight protomers are present in the unit cell and three out of five selenomethionines were found in each protomer using the PHENIX software suite. A full structural determination is in progress to elucidate the structure-function relationship of the protein.
Original language | English |
---|---|
Pages (from-to) | 90-94 |
Number of pages | 5 |
Journal | Acta Crystallographica Section F:Structural Biology Communications |
Volume | 73 |
Issue number | 2 |
DOIs | |
State | Published - 1 Feb 2017 |
Bibliographical note
Publisher Copyright:© 2017 International Union of Crystallography.
Keywords
- Burkholderia pseudomallei
- D-glycero-β-D-manno-heptose-1-phosphate adenylyltransferase
- HldC
- heptose biosynthesis pathway
- melioidosis