Palmgren M G, Buch-Pedersen M J, Møller A L
Department of Plant Biology, The Royal Veterinary and Agricultural University, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Denmark.
Ann N Y Acad Sci. 2003 Apr;986:188-97. doi: 10.1111/j.1749-6632.2003.tb07159.x.
The mechanism of proton pumping by P-type plasma membrane H(+)-ATPases is not well clarified. Site-directed mutagenesis studies suggest that Asp684, situated in transmembrane segment M6, is involved in coordination of proton(s) in plant plasma membrane H(+)-ATPase. This hypothesis is supported by atomic models of H(+)-ATPases built on the basis of the crystal structure of the related SERCA1a Ca(2+)-ATPase. However, more biochemical, genetic, and structural studies are required before we will be able to understand the nature of the proton binding site(s) in P-type H(+)-ATPases and the mechanism of action of these pumps.
P型质膜H(+) - ATP酶质子泵浦机制尚未完全阐明。定点诱变研究表明,位于跨膜片段M6中的天冬氨酸684参与植物质膜H(+) - ATP酶中质子的配位。基于相关的肌浆网Ca(2+) - ATP酶晶体结构构建的H(+) - ATP酶原子模型支持了这一假设。然而,在我们能够理解P型H(+) - ATP酶中质子结合位点的性质以及这些泵的作用机制之前,还需要更多的生物化学、遗传学和结构研究。