Journal
STRUCTURE
Volume 16, Issue 9, Pages 1378-1388Publisher
CELL PRESS
DOI: 10.1016/j.str.2008.05.014
Keywords
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Funding
- Science Foundation Ireland [02-IN1-B266, 07/IN.1/81836]
- National Institutes of Health [GM61070, GM75915]
- National Science Foundation [IIS-0308078, DMR 0225180]
- Enterprise Ireland [CFTD/04/106]
- Ohio State University
- National Institutes of Health
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The crystal structures of the cytoplasmic domain of the putative zinc transporter CzrB in the apo and zinc-bound forms reported herein are consistent with the protein functioning in vivo as a homodimer. NMR, X-ray scattering, and size-exclusion chromatography provide support for dimer formation. Full-length variants of CzrB in the apo and zinc-loaded states were generated by homology modeling with the Zn2+/H+ antiporter YiiP. The model suggests a way in which zinc binding to the cytoplasmic fragment creates a docking site to which a metallochaperone can bind for delivery and transport of its zinc cargo. Because the cytoplasmic domain may exist in the cell as an independent, soluble protein, a proposal is advanced that it functions as a metallochaperone and that it regulates the zinc-transporting activity of the full-length protein. The latter requires that zinc binding becomes uncoupled from the creation of a metallochaperone-docking site on CzrB.
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