Apell H-J
Department of Biology, University of Konstanz, Fach M635, 78457 Konstanz, Germany.
Rev Physiol Biochem Pharmacol. 2003;150:1-35. doi: 10.1007/s10254-003-0018-9. Epub 2003 Jun 17.
P-type ATPases are a large family of membrane proteins that perform active ion transport across biological membranes. In these proteins the energy-providing ATP hydrolysis is coupled to ion-transport that builds up or maintains the electrochemical potential gradients of one or two ion species across the membrane. P-type ATPases are found in virtually all eukaryotic cells and also in bacteria, and they are transporters of a broad variety of ions. So far, a crystal structure with atomic resolution is available only for one species, the SR Ca-ATPase. However, biochemical and biophysical studies provide an abundance of details on the function of this class of ion pumps. The aim of this review is to summarize the results of preferentially biophysical investigations of the three best-studied ion pumps, the Na,K-ATPase, the gastric H,K-ATPase, and the SR Ca-ATPase, and to compare functional properties to recent structural insights with the aim of contributing to the understanding of their structure-function relationship.
P型ATP酶是一类大型膜蛋白，可在生物膜上进行主动离子转运。在这些蛋白质中，提供能量的ATP水解与离子转运相偶联，从而建立或维持一种或两种离子在膜两侧的电化学势梯度。P型ATP酶几乎存在于所有真核细胞以及细菌中，它们是多种离子的转运体。到目前为止，只有一种P型ATP酶（肌浆网Ca-ATP酶）具有原子分辨率的晶体结构。然而，生化和生物物理研究为这类离子泵的功能提供了丰富的细节。本综述的目的是总结对三种研究最为深入的离子泵（钠钾ATP酶、胃质子钾ATP酶和肌浆网Ca-ATP酶）进行的主要生物物理研究结果，并将功能特性与最新的结构见解进行比较，以有助于理解它们的结构-功能关系。
