5XF2

Crystal structure of SeMet-HldC from Burkholderia pseudomallei

5XF2 の概要

• エントリーDOI: 10.2210/pdb5xf2/pdb
• 関連するPDBエントリー: 5X9Q
• 分子名称: Putative cytidylyltransferase, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID (3 entities in total)
• 機能のキーワード: hldc, burkholderia pseudomalle, d-glycero-beta-d-manno-heptose-1-phosphate adenylyltransferase, transferase
• 由来する生物種: Burkholderia pseudomallei (strain K96243)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 152607.86

構造登録者

Park, J.,Kim, H.,Kim, S.,Lee, D.,Shin, D.H. (登録日: 2017-04-07, 公開日: 2017-07-19, 最終更新日: 2024-11-20)

主引用文献

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

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: 28177319
DOI: 10.1107/S2053230X16020537

実験手法

X-RAY DIFFRACTION (2.8 Å)