Picas Laura, Carretero-Genevrier Adrián, Montero M Teresa, Vázquez-Ibar J L, Seantier Bastien, Milhiet Pierre-Emmanuel, Hernández-Borrell Jordi
Departament de Fisicoquímica, Facultat de Farmàcia, Universitat de Barcelona (UB), Spain.
Biochim Biophys Acta. 2010 May;1798(5):1014-9. doi: 10.1016/j.bbamem.2010.01.008. Epub 2010 Jan 21.
We report the insertion of a transmembrane protein, lactose permease (LacY) from Escherichia coli (E. coli), in supported lipid bilayers (SLBs) of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (POPE) and 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol (POPG), in biomimetic molar proportions. We provide evidence of the preferential insertion of LacY in the fluid domains. Analysis of the self-assembled protein arrangements showed that LacY: (i) is inserted as a monomer within fluid domains of SLBs of POPE:POPG (3:1, mol/mol), (ii) has a diameter of approx. 7.8nm; and (iii) keeps an area of phospholipids surrounding the protein that is compatible with shells of phospholipids.
我们报告了来自大肠杆菌（E. coli）的跨膜蛋白乳糖通透酶（LacY）在1-棕榈酰-2-油酰-sn-甘油-3-磷酸乙醇胺（POPE）和1-棕榈酰-2-油酰-sn-甘油-3-磷酸甘油（POPG）的支持脂质双层（SLB）中的插入情况，其比例为仿生摩尔比。我们提供了LacY优先插入流体区域的证据。对自组装蛋白质排列的分析表明，LacY：（i）以单体形式插入POPE:POPG（3:1，摩尔/摩尔）的SLB流体区域内；（ii）直径约为7.8纳米；（iii）在蛋白质周围保留了与磷脂壳相容的磷脂区域。
