TY - JOUR
T1 - Expression and crystallographic studies of D-glycero-b-D-manno-heptose-1-phosphate adenylyltransferase from Burkholderia pseudomallei
AU - Park, Jimin
AU - Kim, Hyojin
AU - Kim, Suwon
AU - Lee, Daeun
AU - Shin, Dong Hae
N1 - Publisher Copyright:
© 2017 International Union of Crystallography.
PY - 2017/2/1
Y1 - 2017/2/1
N2 - 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. 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, α = 108.4, β = 108.4, γ = 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.
AB - 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. 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, α = 108.4, β = 108.4, γ = 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.
KW - Burkholderia pseudomallei
KW - D-glycero-β-D-manno-heptose-1-phosphate adenylyltransferase
KW - HldC
KW - heptose biosynthesis pathway
KW - melioidosis
UR - http://www.scopus.com/inward/record.url?scp=85011982944&partnerID=8YFLogxK
U2 - 10.1107/S2053230X16020537
DO - 10.1107/S2053230X16020537
M3 - Article
C2 - 28177319
AN - SCOPUS:85011982944
VL - 73
SP - 90
EP - 94
JO - Acta Crystallographica Section F:Structural Biology Communications
JF - Acta Crystallographica Section F:Structural Biology Communications
SN - 2053-230X
IS - 2
ER -