Faller Michael, Niederweis Michael, Schulz Georg E
Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Albertstrasse 21, 79104 Freiburg im Breisgau, Germany.
Science. 2004 Feb 20;303(5661):1189-92. doi: 10.1126/science.1094114.
Mycobacteria have low-permeability outer membranes that render them resistant to most antibiotics. Hydrophilic nutrients can enter by way of transmembrane-channel proteins called porins. An x-ray analysis of the main porin from Mycobacterium smegmatis, MspA, revealed a homooctameric goblet-like conformation with a single central channel. This is the first structure of a mycobacterial outer-membrane protein. No structure-related protein was found in the Protein Data Bank. MspA contains two consecutive beta barrels with nonpolar outer surfaces that form a ribbon around the porin, which is too narrow to fit the thickness of the mycobacterial outer membrane in contemporary models.
分枝杆菌具有低渗透性的外膜,这使得它们对大多数抗生素具有抗性。亲水性营养物质可以通过称为孔蛋白的跨膜通道蛋白进入。对耻垢分枝杆菌的主要孔蛋白MspA进行的X射线分析显示,它具有一个中央通道的同八聚体杯状构象。这是分枝杆菌外膜蛋白的首个结构。蛋白质数据库中未发现与该结构相关的蛋白质。MspA包含两个连续的β桶,其非极性外表面围绕孔蛋白形成一条带,在当代模型中,该带太窄,无法容纳分枝杆菌外膜的厚度。