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

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dc.contributor.author Cherezov, Vadim
dc.contributor.author Höfer, Nicole
dc.contributor.author Szebenyi, Doletha M.E.
dc.contributor.author Kolaj-Robin, Olga
dc.contributor.author Wall, J.G.
dc.contributor.author Gillian, Richard
dc.contributor.author Srinivasan, Vasundara
dc.contributor.author Jaroniec, Christopher P.
dc.contributor.author Caffrey, Martin
dc.date.accessioned 2012-07-25T09:21:47Z
dc.date.available 2012-07-25T09:21:47Z
dc.date.issued 2008
dc.identifier.uri http://hdl.handle.net/10344/2403
dc.description peer-reviewed en_US
dc.description This paper was obtained through PEER (Publishing and the Ecology of European Research) http://www.peerproject.eu
dc.description.abstract The crystal structures of the cytoplasmic domain of the putative zinc transporter CzrB in the apoand 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 modelling 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. Since 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. en_US
dc.language.iso eng en_US
dc.publisher Elsevier en_US
dc.relation.ispartofseries Structure;16(9), pp. 1378-1388
dc.relation.uri http://dx.doi.org/10.1016/j.str.2008.05.014
dc.rights This is the author’s version of a work that was accepted for publication in Structure.Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Structure 16(9)pp 1378-1388,http://dx.doi.org/10.1016/j.str.2008.05.014 en_US
dc.subject function en_US
dc.subject high resolution en_US
dc.subject membrane protein en_US
dc.subject metal chaperone en_US
dc.subject x-ray structure en_US
dc.subject YiiP en_US
dc.title Insights into the mode of action of a putative zinc transporter CzrB in thermus thermophilus en_US
dc.type info:eu-repo/semantics/article en_US
dc.type.supercollection all_ul_research en_US
dc.type.supercollection ul_published_reviewed en_US
dc.contributor.sponsor SFI
dc.contributor.sponsor EI
dc.rights.accessrights info:eu-repo/semantics/openAccess en_US


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