Bacterial transition metal P(1B)-ATPases: transport mechanism and roles in virulence.
Bacterial transition metal P(1B)-ATPases: transport mechanism and roles in virulence.
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DOI：
10.1021/bi201418k
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发表时间：
2011-11-22
期刊：
影响因子：
2.9
通讯作者：
Raimunda, Daniel
中科院分区：
文献类型：
--
作者：
Argueello, Jose M.;Gonzalez-Guerrero, Manuel;Raimunda, Daniel
P1B 型 ATP 酶是多位体膜蛋白，它将 ATP 的水解与细胞质过渡金属的流出耦合起来。本文回顾了我们对细菌中这些蛋白质的结构和功能的理解的最新进展。它们是转运 ATP 酶 P 型超家族的成员。 Cu+-ATP 酶是这组转运蛋白中观察最频繁、特征最鲜明的成员。然而，细菌基因组显示出具有一系列底物（Cu+、Zn2+、Co2+）的多种 P1B 型 ATP 酶。此外，由于过渡金属之间的结构相似性，这些蛋白质还可以转运非生理底物（Cu2+、Cd2+、Pb2+、Au+、Ag+）。 P1B 型 ATP 酶具有 6 或 8 个跨膜片段 (TM)，在负责 ATP 结合和水解的胞质结构域侧翼的三个核心 TM 中具有金属配位氨基酸。此外，大多数 P1B 型 ATP 酶中都存在调节性细胞质金属结合域。转运机制的核心是当细胞质底物与伴侣和螯合分子结合时，未络合的金属与这些蛋白质的结合。金属与调节位点的结合是通过分子伴侣和细胞质金属结合域之间的可逆金属交换实现的。相比之下，分子伴侣介导的金属向运输部位的输送似乎是一个基本上不可逆的事件。 P1B-ATP酶具有两个重要的生理功能：维持细胞质金属水平并为金属蛋白的周质组装提供金属。最近的研究表明，这两种作用对于细菌毒力都至关重要，因为 P1B-ATP 酶似乎是克服高吞噬体金属水平的关键，并且是组装周质和分泌金属蛋白所必需的，而这些金属蛋白对于在极端氧化环境中生存至关重要。
P1B-type ATPases are polytopic membrane proteins that couple the hydrolysis of ATP to the efflux of cytoplasmic transition metals. This article reviews recent progress in our understanding of the structure and function of these proteins in bacteria. These are members of the P-type superfamily of transport ATPases. Cu+-ATPases are the most frequently observed and best-characterized members of this group of transporters. However, bacterial genomes show diverse arrays of P1B-type ATPases with a range of substrates (Cu+, Zn2+, Co2+). Furthermore, because of the structural similarities among transitions metals, these proteins can also transport non-physiological substrates (Cu2+, Cd2+, Pb2+, Au+, Ag+). P1B-type ATPases have six or eight transmembrane segments (TM) with metal coordinating amino acids in three core TMs flanking the cytoplasmic domain responsible for ATP binding and hydrolysis. In addition, regulatory cytoplasmic metal binding domains are present in most P1B-type ATPases. Central to the transport mechanism is the binding of the uncomplexed metal to these proteins when cytoplasmic substrates are bound to chaperone and chelating molecules. Metal binding to regulatory sites is through a reversible metal exchange among chaperones and cytoplasmic metal binding domains. In contrast, the chaperone-mediated metal delivery to transport sites appears as a largely irreversible event. P1B-ATPases have two overarching physiological functions: to maintain cytoplasmic metal levels and to provide metals for the periplasmic assembly of metalloproteins. Recent studies have shown that both roles are critical for bacterial virulence, since P1B-ATPases appear key to overcome high phagosomal metal levels and are required for the assembly of periplasmic and secreted metalloproteins that are essential for survival in extreme oxidant environments.
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