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Expression and crystallographic studies of D-glycero-beta-D-manno-heptose-1-phosphate adenylyltransferase from Burkholderia pseudomallei
- Expression and crystallographic studies of D-glycero-beta-D-manno-heptose-1-phosphate adenylyltransferase from Burkholderia pseudomallei
- Park, Jimin; Kim, Hyojin; Kim, Suwon; Lee, Daeun; Shin, Dong Hae
- Ewha Authors
- 신동해; 김수원
- SCOPUS Author ID
- 신동해; 김수원
- Issue Date
- Journal Title
- ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
- vol. 73, pp. 90 - 94
- Burkholderia pseudomallei; heptose biosynthesis pathway; melioidosis; D-glycero-beta-D-manno-heptose-1-phosphate adenylyltransferase; HldC
- INT UNION CRYSTALLOGRAPHY
- SCIE; SCOPUS
- The Gram-negative bacterium Burkholderia pseudomallei is the causative agent of melioidosis. D-glycero-beta-D-manno-Heptose-1-phosphate adenylyltransferase (HldC) is the fourth enzyme of the ADP-L-glycero-beta-D-manno-heptose biosynthesis pathway, which produces an essential carbohydrate comprising the inner core of lipopolysaccharide. Therefore, HldC is a potential target of antibiotics against melioidosis. 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 angstrom resolution. The crystal belonged to the primitive triclinic space group P1, with unit-cell parameters a = 74.0, b = 74.0, c = 74.9 angstrom, alpha = 108.4, beta = 108.4, gamma = 108.0 degrees. 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 structurefunction relationship of the protein.
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