Farci Domenica, Guadalupi Giulia, Bierła Katarzyna, Lobinski Ryszard, Piano Dario
Department of Plant Physiology, Warsaw University of Life Sciences - SGGW, Warsaw, Poland.
Laboratory of Photobiology and Plant Physiology, Department of Life and Environmental Sciences University of Cagliari, Cagliari, Italy.
Front Microbiol. 2019 Jun 28;10:1450. doi: 10.3389/fmicb.2019.01450. eCollection 2019.
Surface (S)-layers are cryptic structures that coat the external surface of the bacterial cell in many species. The paracrystalline regularity of the S-layer is due to the self-assembling of one or more protein units. The property of self-assembling seems to be mediated by specific topologies of the S-layer proteins as well as the presence of specific ions that provide support in building and stabilizing the bi-dimensional S-layer organization. In the present study, we have investigated the self-assembling mechanism of the main S-layer protein of (DR_2577) finding an unusual role played by Fe and Cu in the oligomerization of this protein. These findings may trace a structural and functional metallo-mediated convergence between the role of these metals in the assembling of the S-layer and their well-known roles in protecting against oxidative stress in .
表面（S）层是许多物种中覆盖细菌细胞外表面的隐秘结构。S层的准晶体规则性归因于一种或多种蛋白质单元的自组装。自组装特性似乎由S层蛋白的特定拓扑结构以及特定离子的存在介导，这些离子在构建和稳定二维S层组织中提供支持。在本研究中，我们研究了（DR_2577）主要S层蛋白的自组装机制，发现铁和铜在该蛋白的寡聚化中发挥了不同寻常的作用。这些发现可能描绘出这些金属在S层组装中的作用与其在抵御氧化应激方面的著名作用之间的结构和功能金属介导的趋同。
