Okuda Suguru, Watanabe Shoji, Tokuda Hajime
Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, Japan.
FEBS Lett. 2008 Jun 25;582(15):2247-51. doi: 10.1016/j.febslet.2008.05.022. Epub 2008 May 27.
The structures of a lipoprotein carrier, LolA, and a lipoprotein receptor, LolB, are similar except for an extra C-terminal loop containing a 3(10) helix and beta-strand 12 in LolA. Lipoprotein release was significantly reduced when beta-12 was deleted. Deletion of the 3(10) helix also inhibited the lipoprotein release. Furthermore, lipoproteins were non-specifically localized to membranes when LolA lacked the 3(10) helix. Thus, the membrane localization of lipoproteins with the LolA derivative lacking the 3(10) helix was independent of LolB whereas LolB was essential for the outer membrane localization of lipoproteins with the wild-type LolA.
脂蛋白载体LolA和脂蛋白受体LolB的结构相似，只是LolA在C端有一个额外的环，其中包含一个3(10)螺旋和β链12。当β-12缺失时，脂蛋白的释放显著减少。3(10)螺旋的缺失也抑制了脂蛋白的释放。此外，当LolA缺乏3(10)螺旋时，脂蛋白会非特异性地定位于膜上。因此，缺乏3(10)螺旋的LolA衍生物的脂蛋白的膜定位不依赖于LolB，而LolB对于野生型LolA的脂蛋白在外膜的定位至关重要。
