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

Title
A preliminary X-ray study of sedoheptulose-7-phosphate isomerase from Burkholderia pseudomallei
Authors
Kim M.-S.Shin D.H.
Ewha Authors
신동해
SCOPUS Author ID
신동해scopus
Issue Date
2009
Journal Title
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
ISSN
1744-3091JCR Link
Citation
vol. 65, no. 11, pp. 1110 - 1112
Indexed
SCOPUS WOS scopus
Abstract
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. © 2009 International Union of Crystallography. All rights reserved.
DOI
10.1107/S174430910903259X
Appears in Collections:
약학대학 > 약학과 > Journal papers
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