5XF2
Crystal structure of SeMet-HldC from Burkholderia pseudomallei
Summary for 5XF2
| Entry DOI | 10.2210/pdb5xf2/pdb |
| Related | 5X9Q |
| Descriptor | Putative cytidylyltransferase, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID (3 entities in total) |
| Functional Keywords | hldc, burkholderia pseudomalle, d-glycero-beta-d-manno-heptose-1-phosphate adenylyltransferase, transferase |
| Biological source | Burkholderia pseudomallei (strain K96243) |
| Total number of polymer chains | 8 |
| Total formula weight | 152607.86 |
| Authors | Park, J.,Kim, H.,Kim, S.,Lee, D.,Shin, D.H. (deposition date: 2017-04-07, release date: 2017-07-19, Last modification date: 2024-11-20) |
| Primary citation | Park, J.,Kim, H.,Kim, S.,Lee, D.,Shin, D.H. Expression and crystallographic studies of D-glycero-beta-D-manno-heptose-1-phosphate adenylyltransferase from Burkholderia pseudomallei Acta Crystallogr F Struct Biol Commun, 73:90-94, 2017 Cited by PubMed Abstract: 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. PubMed: 28177319DOI: 10.1107/S2053230X16020537 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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