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3BYR

Mode of Action of a Putative Zinc Transporter CzrB (Zn form)

Summary for 3BYR
Entry DOI10.2210/pdb3byr/pdb
Related3BYP
DescriptorCzrB protein, ZINC ION (3 entities in total)
Functional Keywordsmembrane protein, zinc transporter, transport protein
Biological sourceThermus thermophilus
Total number of polymer chains1
Total formula weight11041.86
Authors
Cherezov, V.,Srinivasan, V.,Szebenyi, D.M.E.,Caffrey, M. (deposition date: 2008-01-16, release date: 2008-09-23, Last modification date: 2024-02-21)
Primary citationCherezov, V.,Hofer, N.,Szebenyi, D.M.,Kolaj, O.,Wall, J.G.,Gillilan, R.,Srinivasan, V.,Jaroniec, C.P.,Caffrey, M.
Insights into the Mode of Action of a Putative Zinc Transporter CzrB in Thermus thermophilus
Structure, 16:1378-1388, 2008
Cited by
PubMed 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.
PubMed: 18786400
DOI: 10.1016/j.str.2008.05.014
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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