Department of Biological Sciences, Purdue University, West Lafayette, IN, 47907, USA.
Interdisciplinary Life Science - PULSe, Purdue University, West Lafayette, IN, 47907, USA.
Commun Biol. 2022 Jan 31;5(1):103. doi: 10.1038/s42003-022-03039-y.
To combat nutritional immunity, N. gonorrhoeae has evolved systems to hijack zinc and other metals directly from host metal-binding proteins such as calprotectin (CP). Here, we report the 6.1 Å cryoEM structure of the gonococcal surface receptor TdfH in complex with a zinc-bound CP tetramer. We further show that TdfH can also interact with CP in the presence of copper and manganese, but not with cobalt.
为了对抗营养免疫，淋病奈瑟菌已经进化出了从宿主金属结合蛋白（如钙卫蛋白）中直接劫持锌和其他金属的系统。在这里，我们报告了 6.1Å 的淋病奈瑟菌表面受体 TdfH 与锌结合的 CP 四聚体复合物的冷冻电镜结构。我们进一步表明，TdfH 可以在存在铜和锰的情况下与 CP 相互作用，但不能与钴相互作用。
