Department of Biomedical Chemistry, The University of Tokyo, Hongo, Bunkyo-ku, Japan.
Mitochondrion. 2009 Nov;9(6):443-53. doi: 10.1016/j.mito.2009.08.004. Epub 2009 Aug 12.
While most protist mitochondrial enzymes could be identified in database, the membrane anchor subunits of Complex II and F(o)F(1)-ATP synthase of malaria parasites are not annotated. Based on the presence of structural fingerprints or proteomics data from other protists, here we present their candidates. In contrast to canonical subunits, Plasmodium Complex II anchors have two transmembrane helices and may coordinate heme b via Tyr in place of His. Transmembrane helix IV of ATP synthase subunit a lacks an essential Arg residue. Membrane anchors of Plasmodium Complex II and ATP synthase are divergent from orthologs and promising targets for new chemotherapeutics.
虽然大多数原生动物的线粒体酶可以在数据库中识别,但疟原虫的复合物 II 和 F(o)F(1)-ATP 合酶的膜锚定亚基没有注释。基于其他原生动物的结构指纹或蛋白质组学数据的存在,我们在这里提出了它们的候选物。与典型的亚基不同,疟原虫复合物 II 的锚定蛋白有两个跨膜螺旋,并且可能通过 Tyr 而不是 His 来协调血红素 b。ATP 合酶亚基 a 的跨膜螺旋 IV 缺少一个必需的 Arg 残基。疟原虫复合物 II 和 ATP 合酶的膜锚定蛋白与同源物不同,是新型化学治疗药物的有前途的靶标。