Expression and crystallographic studies of d-glycero- β -d-manno-heptose-1-phosphate adenylyltransferase from Burkholderia pseudomallei

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.
Source: Acta Crystallographica Section F - Category: Biochemistry Authors: Tags: Burkholderia pseudomallei heptose biosynthesis pathway melioidosis d-glycero- β -d-manno-heptose-1-phosphate adenylyltransferase HldC research communications Source Type: research