Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22908-0733, United States.
Curr Opin Struct Biol. 2017 Oct;46:31-37. doi: 10.1016/j.sbi.2017.05.012. Epub 2017 Jun 10.
Recent advances in cryo-electron microscopy (cryo-EM) have opened up the possibility that a large class of biological structures, helical polymers, may now be readily reconstructed at near-atomic resolution. This will have a huge impact, since most of these structures are unlikely to be crystallized. This review focuses on new cryo-EM studies involving three classes of bacterial pili (chaperone-usher, mating, and Type IV) as well as on archaeal flagellar filaments. While it has long been known that one domain within archaeal flagellar filaments is homologous to a domain within bacterial Type IV pilins, the new studies shed light on how homologous and even highly conserved subunits can pack together in different ways with only small changes in sequence.
近年来,低温电子显微镜(cryo-EM)技术的进步使得一大类生物结构,即螺旋聚合物,现在可以在接近原子分辨率的水平上进行重构。这将产生巨大的影响,因为这些结构中的大多数都不太可能结晶。这篇综述重点介绍了涉及三类细菌菌毛(伴侣菌毛-usher、交配和 IV 型)以及古菌鞭毛丝的新的 cryo-EM 研究。虽然人们早就知道古菌鞭毛丝中的一个结构域与细菌 IV 型菌毛蛋白中的一个结构域同源,但新的研究揭示了同源甚至高度保守的亚基如何在只有微小序列变化的情况下以不同的方式包装在一起。