Structural and functional characterizations of the C-terminal domains of CzcD proteins
| Autor: | Christopher A. McDevitt, Monique Fatmous, Ghruta Purohit, Christian Spehar, Katherine Ganio, Megan J. Maher, Daniel M. La Porta, Matthew J.A. Hein, Saumya R. Udagedara, G Patricia Casas Garcia |
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| Rok vydání: | 2020 |
| Předmět: |
biology
Bacteria 010405 organic chemistry Cupriavidus metallidurans Chemistry Metal ion transport Protein domain 010402 general chemistry biology.organism_classification 01 natural sciences Biochemistry 0104 chemical sciences Transport protein Inorganic Chemistry Structure-Activity Relationship Bacterial Proteins Protein Domains Thermotoga maritima bacteria Efflux Shewanella oneidensis Cation Transport Proteins Cation diffusion facilitator |
| Zdroj: | Journal of inorganic biochemistry. 208 |
| ISSN: | 1873-3344 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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