3BYP

Mode of Action of a Putative Zinc Transporter CzrB

Summary for 3BYP

• Entry DOI: 10.2210/pdb3byp/pdb
• Related: 3BYR
• Descriptor: CzrB protein, SULFATE ION (3 entities in total)
• Functional Keywords: membrane protein, zinc transporter, transport protein
• Biological source: Thermus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 21848.63

Authors

Cherezov, V.,Srinivasan, V.,Szebenyi, D.M.E.,Caffrey, M. (deposition date: 2008-01-16, release date: 2008-09-23, Last modification date: 2024-04-03)

Primary citation

Cherezov, 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

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

Experimental method

X-RAY DIFFRACTION (1.7 Å)