A preliminary X-ray study of transketolase from Burkholderia pseudomallei

Mi Sun Kim, Areum Lim, Seung Won Yang, Daeun Lee, Jimin Park, Dong Hae Shin

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


ATktA 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-β-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 A resolution. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a = 146.2, b = 74.6, c = 61.6 A, β = 113.0°. A full structural determination is under way in order to provide insight into the structure-function relationship of this protein.

Original languageEnglish
Pages (from-to)1554-1556
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number12
StatePublished - Dec 2012


  • Burkholderia pseudomallei
  • Tkt
  • transketolase


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