| Literature DB >> 20096263 |
Laura Picas1, Adrián Carretero-Genevrier, M Teresa Montero, J L Vázquez-Ibar, Bastien Seantier, Pierre-Emmanuel Milhiet, Jordi Hernández-Borrell.
Abstract
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. 2009 Elsevier B.V. All rights reserved.Entities:
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Year: 2010 PMID： 20096263 DOI： 10.1016/j.bbamem.2010.01.008
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002