A preliminary X-ray study of transketolase from Burkholderia pseudomallei.

ABSTRACT: TktA is the most critical enzyme in the nonoxidative pentose phosphate pathway. It catalyzes the conversion of xylulose 5-phosphate and ribose 5-phosphate into sedoheptulose 7-phosphate and glyceraldehyde 3-phosphate, and its products are used in the biosynthesis of acetyl-CoA, aromatic amino acids, nucleic acids and ADP-L-glycero-?-D-manno-heptose. TktA also has an unexpected role in chromosome structure that is independent of its metabolic responsibilities. Therefore, it is a new potent antibiotic target. In this study, TktA from Burkholderia pseudomallei has been cloned, expressed, purified and crystallized. Synchrotron X-ray data were also collected to 2.0?Å resolution. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a=146.2, b=74.6, c=61.6?Å, ?=113.0°. A full structural determination is under way in order to provide insight into the structure-function relationship of this protein.

SUBMITTER: Kim MS 

PROVIDER: S-EPMC3509987 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature