Structural and functional characterizations of the C-terminal domains of CzcD proteins
Saumya R Udagedara, Daniel M La Porta, Christian Spehar, Ghruta Purohit, Matthew JA Hein, Monique E Fatmous, G Patricia Casas Garcia, Katherine Ganio, Christopher A McDevitt, Megan J Maher
JOURNAL OF INORGANIC BIOCHEMISTRY | ELSEVIER SCIENCE INC | Published : 2020
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 re..View full abstract
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Awarded by Australian Research Council (ARC)
Awarded by National Health and Medical Research Council (NHMRC)
This research was funded by Australian Research Council (ARC) Discovery Project Grant DP170102102 to CAM and Future Fellowships to MJM (FT180100397) and CAM (FT170100006). This work was also supported by the National Health and Medical Research Council (NHMRC) Project Grants GNT1080784 and GNT1140554 to MJM and CAM. Part of this study was carried out using the MX2 beamline at the Australian Synchrotron, with is part of ANSTO, and made use of the ACRF detector. We thank the beamline staff for their enthusiastic and professional support. We thank Dr. Yee-Foong Mok at the Melbourne Protein characterization facility, The Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne for performing the AUC experiments and data analyses.