Crystal structure of Sa240: A ribose pyranase homolog with partial active site from Staphylococcus aureus
作者: Ling WangMinhao WuJianye Zang
作者单位: 1School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, People’s Republic of China
刊名: Journal of Structural Biology, 2011, Vol.174 (2), pp.413-419
来源数据库: Elsevier Journal
DOI: 10.1016/j.jsb.2011.01.007
关键词: Ribose pyranaseSa240Staphylococcus aureusCrystal structureRbsD homologRibose
英文摘要: Abstract(#br)Ribose is transported into cells in its pyranose form and must be rearranged to its furanose form for further utilization. Ribose pyranase RbsD catalyzes the conversion of ribose from the pyranose to furanose form. This is the key step for substrate supply to ribokinase RbsK, which converts ribose to ribose-5-phosphate for further metabolism. Sequence analysis indicated Sa240 from Staphylococcus aureus was a ribose pyranase homolog. Here we showed that Sa240 formed dimeric structure both in solution and in crystal. S240-ribose complex structure showed a ribose binding site formed by an incomplete active site compared with RbsD. Because the catalytic activity of ribose pyranase depends on its oligomeric state, we propose Sa240 is catalytically inactive in its dimeric structure.
全文获取路径: Elsevier  (合作)
影响因子:3.361 (2012)

  • ribose 核糖
  • homolog 同系物
  • structure 构造
  • partial 局部的
  • active 活动的