Molecular basis of substrate-induced permeation by an amino acid antiporter
作者: Lukasz KowalczykMercè RateraAntonella PaladinoPaola BartoccioniEkaitz Errasti-MurugarrenEva ValenciaGuillem PortellaSusanna BialAntonio ZorzanoIgnacio FitaModesto OrozcoXavier CarpenaJosé Luis Vázquez-lbarManuel PalacínH. Ronald Kaback
刊名: Proceedings of the National Academy of Sciences of the United States of America, 2011, Vol.108 (10), pp.3935-3940
来源数据库: JSTOR
原始语种摘要: Transporters of the amino acid, polyamine and organocation (APC) superfamily play essential roles in cell redox balance, cancer, and aminoacidurias. The bacterial L-arginine/agmatine antiporter, AdiC, is the main APC structural paradigm and shares the "5 + 5 inverted repeat" fold found in other families like the Na⁺ -coupled neurotransmitter transporters. The available AdiC crystal structures capture two states of its transport cycle: the open-to-out apo and the outward-facing Arg⁺ -bound occluded. However, the role of Arg⁺ during the transition between these two states remains unknown. Here, we report the crystal structure at 3.0 Å resolution of an Arg⁺ -bound AdiC mutant (N101A) in the opento-out conformation, completing the picture of the major conformational states during the...
全文获取路径: JSTOR  (合作)

  • substrate 基质
  • induced 感应的
  • permeation 渗透
  • crystal 晶体
  • coordination 配位
  • structure 构造
  • between 在中间
  • balance 平衡
  • mobility 活动性
  • current