ISBN-13: 9783639136708 / Angielski / Miękka / 2009 / 92 str.
Highly solved crystal structures and a wealth ofbiochemical data are now available for an increasingnumber of membrane proteins. However, the question ofhow lipid molecules interact with integral membraneproteins and regulate their structure and function inbiological membranes remains unsatisfactorily addressed. This book discusses the functional mechanismsof membrane proteins in general and the effect of thesurrounding lipidic environment, in the context ofrecent developments in the field. Recent experimentalinvestigations on the proton gradient-drivenmultidrug transporter LmrP are also discussed. Usingthis membrane protein as a model, we demonstratedthat the protein structure and function was dependingon the phosphatidylethanolamine (PE) headgroup. Wethen showed that a negatively charged residue, Asp68,could participate in the interaction with PE and thatsuch interaction is required for proper activity andstructure of the protein. Because Asp-68 belongs to ahighly conserved motif of the Major FacilitatorSuperfamily (MFS) , this interaction might be ageneral feature of these transporters that isinvolved in proton gradient sensing and lipid dependence.