Invited review: Mechanisms of GTP hydrolysis and conformational transitions in the dynamin superfamily.
Invited review: Mechanisms of GTP hydrolysis and conformational transitions in the dynamin superfamily.
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DOI：
10.1002/bip.22855
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发表时间：
2016-08
期刊：
影响因子：
2.9
通讯作者：
Praefcke, Gerrit J. K.
中科院分区：
文献类型：
--
作者：
Daumke, Oliver;Praefcke, Gerrit J. K.
动力蛋白超家族蛋白是多结构域机械化学gtp酶，与核苷酸依赖性膜重塑事件有关。这些蛋白的一个显著特征是它们的组装刺激GTP水解机制。该反应的分子基础已经初步阐明了动力蛋白相关鸟苷酸结合蛋白1 (GBP1)，并涉及GTPase结构域以平行头对头方式的瞬时二聚化。来自磷酸结合（P‐）环的催化精氨酸手指被重新定位到相同分子的核苷酸上，以稳定GTP水解的过渡状态。Dynamin使用相关的二聚化依赖机制，但不是催化精氨酸，而是一价阳离子参与催化。还有另一种GTP水解机制的变化已经被揭示出来，如在P环的相应位置上带有甘氨酸的类似动力蛋白的Irga6。在这里，我们强调了动力蛋白超家族蛋白中GTP水解的保守性和差异性特征，并展示了核苷酸结合和水解如何转化为机械化学运动。我们还描述了如何利用GTP水解的能量进行各种膜重构事件的模型，如膜裂变或融合。©2016 Wiley期刊公司生物工程学报（英文版），2016。
Dynamin superfamily proteins are multidomain mechano‐chemical GTPases which are implicated in nucleotide‐dependent membrane remodeling events. A prominent feature of these proteins is their assembly‐ stimulated mechanism of GTP hydrolysis. The molecular basis for this reaction has been initially clarified for the dynamin‐related guanylate binding protein 1 (GBP1) and involves the transient dimerization of the GTPase domains in a parallel head‐to‐head fashion. A catalytic arginine finger from the phosphate binding (P‐) loop is repositioned toward the nucleotide of the same molecule to stabilize the transition state of GTP hydrolysis. Dynamin uses a related dimerization‐dependent mechanism, but instead of the catalytic arginine, a monovalent cation is involved in catalysis. Still another variation of the GTP hydrolysis mechanism has been revealed for the dynamin‐like Irga6 which bears a glycine at the corresponding position in the P‐loop. Here, we highlight conserved and divergent features of GTP hydrolysis in dynamin superfamily proteins and show how nucleotide binding and hydrolysis are converted into mechano‐chemical movements. We also describe models how the energy of GTP hydrolysis can be harnessed for diverse membrane remodeling events, such as membrane fission or fusion. © 2016 Wiley Periodicals, Inc. Biopolymers 105: 580–593, 2016.
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