ORGANIZATION OF P-TYPE ATPASES - SIGNIFICANCE OF STRUCTURAL DIVERSITY
ORGANIZATION OF P-TYPE ATPASES - SIGNIFICANCE OF STRUCTURAL DIVERSITY
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DOI：
10.1021/bi00048a001
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发表时间：
1995-12-05
期刊：
影响因子：
2.9
通讯作者：
KAPLAN, JH
中科院分区：
文献类型：
--
作者：
LUTSENKO, S;KAPLAN, JH
P型ATPase形成了一个由50多种膜蛋白组成的大家族，负责各种阳离子在细胞膜上的主动运输。阳离子相对于其电化学势梯度的移位是利用三磷酸腺苷末端磷酸键的水解能实现的。不变序列DKTG中天冬氨酸在周转过程中的磷酸化是P型ATPase区别于V型ATPase和F0Fi-ATPase的区别。本文着重讨论了P型ATPase的结构多样性，并将P型ATPase分子的一般结构与阳离子转运类型联系起来。ATPase之间的结构差异以及运输阳离子性质的显著差异表明，不同阳离子转移的分子机制细节并不相同。目前，关于大多数新发现的ATPase的性质的实验数据很少，显然，关于它们结构和机制中的共性的假设需要彻底的测试。特别是，我们希望表明，目前关于P型ATPase结构组织的观点需要重新评估，以使共同整体机制的想法与其结构多样性相一致。
The P-type ATPases form a large family of more than 50 membrane proteins, which are responsible for the active transport of a variety of cations across cell membranes. Translocation of cations against their electrochemical po-tential gradient is achievedby utilizing the energy of hydrolysis of the terminal phosphate bond of ATP. Phos-phorylation of the aspartic acidin the invariant sequence DKTG during turnover distinguishes P-type ATPases from V-type and F0Fi-ATPases. This article is focused on the structural diversity among P-type ATPases, and it relates the general organization of the P-type ATPasemolecule to the type of transported cation. Structural variations among the ATPases as well as striking differences in the properties of transported cations suggest that details of the molecular mechanisms underlying the translocation of different cations are not identical. Presently little experimental data are available on properties of the majority of the newly discovered ATPases, and it is evident that assumptions regarding commonality in their structures and mechanisms require thorough testing. In particular, we hope to show that current views on structural organization of P-type ATPases require reassessment in order to reconcile the idea of common overall mechanism with their structural diversity.