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Lipids in the structure, folding, and function of the KcsA K+ channel
Author(s): Valiyaveetil FI, Zhou YF, Mackinnon R
Source: BIOCHEMISTRY    Volume: 41    Issue: 35    Pages: 10771-10777    Published: SEP 3 2002  
Times Cited: 121     References: 33     
Abstract: Lipid molecules surround an ion channel in its native environment of cellular membranes. The importance of the lipid bilayer and the role of lipid protein interactions in ion channel structure and function are not well understood. Here we demonstrate that the bacterial potassium channel KcsA binds a negatively charged lipid molecule. We have defined the potential binding site of the lipid molecule on KcsA by X-ray crystallographic analysis of a complex of KcsA with a monoclonal antibody Fab fragment. We also demonstrate that lipids are required for the in vitro refolding of the KcsA tetramer from the unfolded monomeric state. The correct refolding of the KcsA tetramer requires lipids, but it is not dependent on negatively charged lipids as refolding takes place in the absence of such lipids. We confirm that the presence of negatively charged lipids is required for ion conduction through the KcsA potassium channel, suggesting that the lipid bound to KcsA is important for ion channel function.
Document Type: Article
Language: English
Reprint Address: Mackinnon, R (reprint author), Rockefeller Univ, Howard Hughes Med Inst, Lab Mol Neurobiol & Biophys, 1230 York Ave, New York, NY 10021 USA
Addresses:
1. Rockefeller Univ, Howard Hughes Med Inst, Lab Mol Neurobiol & Biophys, New York, NY 10021 USA
Publisher: AMER CHEMICAL SOC, 1155 16TH ST, NW, WASHINGTON, DC 20036 USA
Subject Category: Biochemistry & Molecular Biology
IDS Number: 589ET
ISSN: 0006-2960
DOI: 10.1021/b0206215y
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