A preliminary X-ray study of sedoheptulose-7-phosphate isomerase from Burkholderia pseudomallei

Mi Sun Kim, Dong Hae Shin

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3 Scopus citations


Sedoheptulose-7-phosphate isomerase (GmhA) converts d-sedoheptulose 7 - phosphate to d,d-heptose 7-phosphate. This is the first step in the biosynthesis pathway of NDP-heptose, which is responsible for the pleiotropic phenotype. This biosynthesis pathway is the target of inhibitors to increase the membrane permeability of Gram-negative pathogens or of adjuvants working synergistically with known antibiotics. Burkholderia pseudomallei is the causative agent of melioidosis, a seriously invasive disease in animals and humans in tropical and subtropical areas. GmhA from B. pseudomallei is one of the targets of antibiotic adjuvants for melioidosis. In this study, GmhA has been cloned, expressed, purified and crystallized. Synchrotron X-ray data were also collected to 1.9 Å resolution. The crystal belonged to the primitive orthorhombic space group P212121, with unit-cell parameters a = 61.3, b = 84.2, c = 142.3 Å. A full structural determination is under way in order to provide insights into the structure-function relationships of this protein.

Original languageEnglish
Pages (from-to)1110-1112
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number11
StatePublished - 2009


  • Burkholderia pseudomallei
  • Sedoheptulose-7-phosphate isomerase


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