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Type: Journal article
Title: Structural and functional characterizations of the C-terminal domains of CzcD proteins
Author: 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.
Citation: Journal of Inorganic Biochemistry, 2020; 208:111087-1-111087-9
Publisher: Elsevier
Issue Date: 2020
ISSN: 0162-0134
Statement of
Saumya R. Udagedara, Daniel M. La Porta, Christian Spehar, Ghruta Purohit, Matthew J.A. Hein, Monique E. Fatmous, G. Patricia Casas Garcia, Katherine Ganio, Christopher A. McDevitt, Megan J. Maher
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.
Keywords: Cation diffusion facilitator protein (CDF); CzcD; zinc; analytical ultracentrifugation (AUC); isothermal titration calorimetry (ITC); X-ray crystallography
Rights: © 2020 Elsevier Inc. All rights reserved.
DOI: 10.1016/j.jinorgbio.2020.111087
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Microbiology and Immunology publications

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