MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, United Kingdom.
Curr Opin Struct Biol. 2010 Dec;20(6):791-8. doi: 10.1016/j.sbi.2010.09.011. Epub 2010 Oct 21.
Dynamins form a family of eukaryotic and prokaryotic proteins involved in membrane fission, fusion and restructuring. They have complex mechanisms of self-assembly, which are coupled to the tubulation and destabilization of lipid bilayers. Recent structural data has revolutionized our understanding and is now yielding detailed insights into dynamin structure, from monomer through to polymer. Traditional division of the dynamin subunit into GTPase domain, middle domain and GTPase effector domain based on sequence alignments and biochemistry is not supported by recent structural data. A unified model of dynamin architecture is presented here, based on observation that the basic dynamin fold is conserved across evolutionary kingdoms.
动力蛋白是一类真核和原核蛋白，参与膜的分裂、融合和重构。它们具有复杂的自组装机制，与脂质双层的管状化和去稳定化相关联。最近的结构数据彻底改变了我们的认识，并为我们提供了有关动力蛋白结构的详细见解，从单体到聚合物。基于序列比对和生物化学的传统动力蛋白亚基划分，即 GTP 酶结构域、中间结构域和 GTP 酶效应结构域，最近的结构数据并不支持。本文提出了一种统一的动力蛋白结构模型，基于这样的观察，即基本的动力蛋白折叠在进化领域中是保守的。
