6VD9

Metal-bound C-terminal domain of the CzcD transporter from Cuprividus metallidurans

Summary for 6VD9

• Entry DOI: 10.2210/pdb6vd9/pdb
• Descriptor: Metal cation efflux system protein CzcD, NICKEL (II) ION (3 entities in total)
• Functional Keywords: cation diffusion facilitator protein (cdf), czcd, transport protein
• Biological source: Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)
• Total number of polymer chains: 4
• Total formula weight: 33684.82

Authors

Maher, M.J. (deposition date: 2019-12-23, release date: 2020-06-24, Last modification date: 2023-10-11)

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

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: 32505855
DOI: 10.1016/j.jinorgbio.2020.111087

Experimental method

X-RAY DIFFRACTION (1.75 Å)