Paramagnetic Relaxation Enhancement Reveals Oligomerization Interface of a Membrane Protein

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• 作者：Shenlin Wang ; Rachel A. Munro ; So Young Kim ; Kwang-Hwan Jung ; Leonid S. Brown ; Vladimir Ladizhansky
• 刊名：The Journal of the American Chemical Society
• 出版年：2012
• 出版时间：October 17, 2012
• 年：2012
• 卷：134
• 期：41
• 页码：16995-16998
• 全文大小：280K
• 年卷期：v.134,no.41(October 17, 2012)
• ISSN：1520-5126

文摘

Protein鈥損rotein interactions play critical roles in cellular function and oligomerization of membrane proteins is a commonly observed phenomenon. Determining the oligomerization state and defining the intermolecular interface in the bilayer is generally a difficult task. Here, we use site-specific spin labeling to demonstrate that relaxation enhancements induced by covalently attached paramagnetic tag can provide distance restraints defining the intermonomer interface in oligomers formed by a seven-helical transmembrane protein Anabaena Sensory Rhodopsin (ASR). We combine these measurements with visible CD spectroscopy and cross-linking experiments to demonstrate that ASR forms tight trimers in both detergents and lipids.