Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1798, Issue 5, Pages 1014-1019Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2010.01.008
Keywords
Lactose permease; AFM; Phospholipid domains
Categories
Funding
- University of Barcelona
- Hispano-French bilateral action [HF 2007-0028]
- Spanish Government [CTQ-2008-03922/BQU]
- ANR PCV [AFM-MB-PROT]
- ICREA Funding Source: Custom
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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 1palmitoy1-2-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. 7.8 nm; and (iii) keeps an area of phospholipids surrounding the protein that is compatible with shells of phospholipids. (C) 2010 Elsevier B.V. All rights reserved.
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