Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne 3083, Australia.
Department of Microbiology and Immunology, The Peter Doherty Institute for Infection and Immunity, The University of Melbourne, Melbourne 3000, Australia.
J Inorg Biochem. 2020 Jul;208:111087. doi: 10.1016/j.jinorgbio.2020.111087. Epub 2020 Apr 23.
Zinc is a potent antimicrobial component of the innate immune response at the host-pathogen interface. Bacteria subvert or resist host zinc insults by metal efflux pathways that include cation diffusion facilitator (CDF) proteins. The structural and functional examination of this protein class has been limited, with only the structures of the zinc transporter YiiP proteins from E. coli and Shewanella oneidensis described to date. Here, we determine the metal binding properties, solution quaternary structures and three dimensional architectures of the C-terminal domains of the metal transporter CzcD proteins from Cupriavidus metallidurans, Pseudomonas aeruginosa and Thermotoga maritima. We reveal significant diversity in the metal-binding properties and structures of these proteins and discover a potential novel mechanism for metal-promoted dimerization for the Cupriavidus metallidurans and Pseudomonas aeruginosa proteins.
锌是宿主-病原体界面先天免疫反应中的一种有效的抗菌成分。细菌通过金属外排途径来颠覆或抵抗宿主的锌胁迫，其中包括阳离子扩散促进剂（CDF）蛋白。该蛋白类别的结构和功能研究受到限制，迄今为止仅描述了来自大肠杆菌和希瓦氏菌的锌转运蛋白 YiiP 蛋白的结构。在这里，我们确定了金属转运蛋白 CzcD 蛋白的金属结合特性、溶液四级结构和三维结构，这些蛋白来自铜绿假单胞菌、嗜热栖热菌和铜绿假单胞菌。我们揭示了这些蛋白质在金属结合特性和结构上的显著多样性，并发现了铜绿假单胞菌和铜绿假单胞菌蛋白中金属促进二聚化的潜在新机制。
