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Structure. 2008 Sep 10;16(9):1378-88. doi: 10.1016/j.str.2008.05.014.

Insights into the mode of action of a putative zinc transporter CzrB in Thermus thermophilus.

Author information

1
Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

Abstract

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.

PMID:
18786400
PMCID:
PMC2614558
DOI:
10.1016/j.str.2008.05.014
[Indexed for MEDLINE]
Free PMC Article

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