5xf2
From Proteopedia
Crystal structure of SeMet-HldC from Burkholderia pseudomallei
Structural highlights
FunctionQ63XZ4_BURPS Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.[SAAS:SAAS00558028] Publication Abstract from PubMedThe 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 A resolution. The crystal belonged to the primitive triclinic space group P1, with unit-cell parameters a = 74.0, b = 74.0, c = 74.9 A, 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 structure-function relationship of the protein. Expression and crystallographic studies of D-glycero-beta-D-manno-heptose-1-phosphate adenylyltransferase from Burkholderia pseudomallei.,Park J, Kim H, Kim S, Lee D, Shin DH Acta Crystallogr F Struct Biol Commun. 2017 Feb 1;73(Pt 2):90-94. doi:, 10.1107/S2053230X16020537. Epub 2017 Jan 19. PMID:28177319[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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