Center for Biomembrane Research and Stockholm Bioinformatics Center, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.
J Mol Biol. 2010 Mar 19;397(1):190-201. doi: 10.1016/j.jmb.2010.01.042. Epub 2010 Jan 25.
We have determined the optimal placement of individual transmembrane helices in the Pyrococcus horikoshii Glt(Ph) glutamate transporter homolog in the membrane. The results are in close agreement with theoretical predictions based on hydrophobicity, but do not, in general, match the known three-dimensional structure, suggesting that transmembrane helices can be repositioned relative to the membrane during folding and oligomerization. Theoretical analysis of a database of membrane protein structures provides additional support for this idea. These observations raise new challenges for the structure prediction of membrane proteins and suggest that the classical two-stage model often used to describe membrane protein folding needs to be modified.
我们已经确定了 Pyrococcus horikoshii Glt(Ph) 谷氨酸转运蛋白同源物在膜中的各个跨膜螺旋的最佳位置。这些结果与基于疏水性的理论预测非常吻合，但通常与已知的三维结构不匹配，这表明跨膜螺旋在折叠和寡聚化过程中可以相对于膜重新定位。对膜蛋白结构数据库的理论分析为这一观点提供了额外的支持。这些观察结果为膜蛋白的结构预测提出了新的挑战，并表明常用于描述膜蛋白折叠的经典两阶段模型需要进行修改。
