MOVEMENT AND SELF-CONTROL IN PROTEIN ASSEMBLIES - QUASI-EQUIVALENCE REVISITED
MOVEMENT AND SELF-CONTROL IN PROTEIN ASSEMBLIES - QUASI-EQUIVALENCE REVISITED
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DOI：
10.1016/s0006-3495(80)84929-0
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发表时间：
1980-01-01
影响因子：
3.4
通讯作者：
CASPAR, DLD
中科院分区：
文献类型：
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作者：
CASPAR, DLD
不同构象状态之间有目的的转换在蛋白质组装体的构建和作用中发挥自我控制作用。拟等价性是用来解释二十面体病毒结构的，它是通过将相同的蛋白质亚基分化为不同的构象而产生的，这些构象保留了基本的键合特异性。机械模型旨在代表结构中的能量分布，而不仅仅是物质的排列，用于探索病毒粒子的灵活性和自我控制运动。关于细菌鞭毛、肌动蛋白、烟草花叶病毒和T4噬菌体尾部结构的组装的信息表明，组装可以通过将亚基从非活性的、不社会的形式转换为活性的、可缔合的形式来控制。驱动这种变化的能量是由生长结构中的亚基间键合提供的;这种通过构象转换进行的组装的自我控制被称为“autostery”，与变构同源。一个机械模型的收缩T4尾鞘已被构建，以证明如何自我控制激活的潜在的键合电位可以驱动一个有目的的运动。在收缩尾鞘中模拟的准等效构象梯度为尾管长度的自我决定提出了一个可行的机制。由相同蛋白质组装而成的协同作用通常取决于个体差异化的运动。
Purposeful switching among different conformational states exerts self-control in the construction and action of protein assemblies. Quasi-equivalence, conceived to explain icosahedral virus structure, arises by differentiation of identical protein subunits into different conformations that conserve essential bonding specificity. Mechanical models designed to represent the energy distribution in the structure, rather than just the arrangement of matter, are used to explore flexibility and self-controlled movements in virus particles. Information about the assembly of bacterial flagella, actin, tobacco mosaic virus and the T4 bacteriophage tail structure show that assembly can be controlled by switching the subunits from an inactive, unsociable form to an active, associable form. Energy to drive this change is provided by the intersubunit bonding in the growing structure; this self-control of assembly by conformational switching is called "autostery", by homology with allostery. A mechanical model of the contractile T4 tail sheath has been constructed to demonstrate how self-controlled activation of a latent bonding potential can drive a purposeful movement. The gradient of quasi-equivalent conformations modelled in the contracting tail sheath has suggested a workable mechanism for self-determination of tail tube length. Concerted action by assemblies of identical proteins may often depend on individually differentiated movements.