6VD8
Metal-bound C-terminal domain of CzcD transporter from Pseudomonas aeruginosa
Summary for 6VD8
Entry DOI | 10.2210/pdb6vd8/pdb |
Descriptor | Probable cation efflux system protein, ZINC ION (3 entities in total) |
Functional Keywords | cation diffusion facilitator protein (cdf), czcd, transport protein |
Biological source | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
Total number of polymer chains | 2 |
Total formula weight | 18708.02 |
Authors | Maher, M.J. (deposition date: 2019-12-23, release date: 2020-06-24, Last modification date: 2024-03-06) |
Primary citation | Udagedara, S.R.,La Porta, D.M.,Spehar, C.,Purohit, G.,Hein, M.J.A.,Fatmous, M.E.,Casas Garcia, G.P.,Ganio, K.,McDevitt, C.A.,Maher, M.J. Structural and functional characterizations of the C-terminal domains of CzcD proteins. J.Inorg.Biochem., 208:111087-111087, 2020 Cited by PubMed Abstract: 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. PubMed: 32505855DOI: 10.1016/j.jinorgbio.2020.111087 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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