Encinar J A, Molina M L, Poveda J A, Barrera F N, Renart M L, Fernández A M, González-Ros J M
Instituto de Biología Molecular y Celular, Universidad Miguel Hernández, Elche, 03202 Alicante, Spain.
FEBS Lett. 2005 Sep 26;579(23):5199-204. doi: 10.1016/j.febslet.2005.08.038.
The lack of a membrane environment in membrane protein crystals is considered one of the major limiting factors to fully imply X-ray structural data to explain functional properties of ion channels [Gulbis, J.M. and Doyle, D. (2004) Curr. Opin. Struct. Biol. 14, 440-446]. Here, we provide infrared spectroscopic evidence that the structure and stability of the potassium channel KcsA and its chymotryptic derivative 1-125 KcsA reconstituted into native-like membranes differ from those exhibited by these proteins in detergent solution, the latter taken as an approximation of the mixed detergent-protein crystal conditions.
膜蛋白晶体中缺乏膜环境被认为是充分利用X射线结构数据来解释离子通道功能特性的主要限制因素之一[Gulbis, J.M.和Doyle, D. (2004) Curr. Opin. Struct. Biol. 14, 440 - 446]。在此，我们提供红外光谱证据表明，重构到类天然膜中的钾通道KcsA及其胰凝乳蛋白酶衍生体1 - 125 KcsA的结构和稳定性与这些蛋白质在去污剂溶液中的情况不同，后者被视为混合去污剂 - 蛋白质晶体条件的近似情况。
