6vda

Publication Abstract from PubMed

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.

Structural and functional characterizations of the C-terminal domains of CzcD proteins.,Udagedara SR, La Porta DM, Spehar C, Purohit G, Hein MJA, Fatmous ME, Casas Garcia GP, Ganio K, McDevitt CA, Maher MJ J Inorg Biochem. 2020 Jul;208:111087. doi: 10.1016/j.jinorgbio.2020.111087. Epub , 2020 Apr 23. PMID:32505855^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.