Unknown

Dataset Information

0

Expression and crystallographic studies of D-glycero-?-D-manno-heptose-1-phosphate adenylyltransferase from Burkholderia pseudomallei.


ABSTRACT: The Gram-negative bacterium Burkholderia pseudomallei is the causative agent of melioidosis. D-glycero-?-D-manno-Heptose-1-phosphate adenylyltransferase (HldC) is the fourth enzyme of the ADP-L-glycero-?-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?Å resolution. The crystal belonged to the primitive triclinic space group P1, with unit-cell parameters a = 74.0, b = 74.0, c = 74.9?Å, ? = 108.4, ? = 108.4, ? = 108.0°. 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 structure-function relationship of the protein.

SUBMITTER: Park J 

PROVIDER: S-EPMC5297929 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

Expression and crystallographic studies of D-glycero-β-D-manno-heptose-1-phosphate adenylyltransferase from Burkholderia pseudomallei.

Park Jimin J   Kim Hyojin H   Kim Suwon S   Lee Daeun D   Shin Dong Hae DH  

Acta crystallographica. Section F, Structural biology communications 20170119 Pt 2


The Gram-negative bacterium Burkholderia pseudomallei is the causative agent of melioidosis. D-glycero-β-D-manno-Heptose-1-phosphate adenylyltransferase (HldC) is the fourth enzyme of the ADP-L-glycero-β-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  ...[more]

Similar Datasets

| S-EPMC7993394 | biostudies-literature
| S-EPMC1196024 | biostudies-literature
| S-EPMC3585733 | biostudies-literature
| S-EPMC6981941 | biostudies-literature
| S-EPMC7411327 | biostudies-literature
| S-EPMC3169398 | biostudies-literature
| S-EPMC2844805 | biostudies-literature
| S-EPMC3976583 | biostudies-literature
| S-EPMC4259243 | biostudies-literature
| S-EPMC2844806 | biostudies-literature