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A structural overview of the zinc transporters in the cation diffusion facilitator family
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Number of Authors: 42019 (English)In: Acta Crystallographica Section D Structural Biology, ISSN 2059-7983, Vol. 75, p. 357-367Article, review/survey (Refereed) Published
Abstract [en]

The cation diffusion facilitators (CDFs) are a family of membrane-bound proteins that maintain cellular homeostasis of essential metal ions. In humans, the zinc-transporter CDF family members (ZnTs) play important roles in zinc homeostasis. They do this by facilitating zinc efflux from the cytoplasm to the extracellular space across the plasma membrane or into intracellular organelles. Several ZnTs have been implicated in human health owing to their association with type 2 diabetes and neurodegenerative diseases. Although the structure determination of CDF family members is not trivial, recent advances in membrane-protein structural biology have resulted in two structures of bacterial YiiPs and several structures of their soluble C-terminal domains. These data reveal new insights into the molecular mechanism of ZnT proteins, suggesting a unique rocking-bundle mechanism that provides alternating access to the metal-binding site.

Place, publisher, year, edition, pages
2019. Vol. 75, p. 357-367
Keywords [en]
cation diffusion facilitator, membrane proteins, zinc transporter
National Category
Biological Sciences Chemical Sciences
Identifiers
URN: urn:nbn:se:su:diva-168635DOI: 10.1107/S2059798319003814ISI: 000464641700001PubMedID: 30988253OAI: oai:DiVA.org:su-168635DiVA, id: diva2:1314029
Available from: 2019-05-07 Created: 2019-05-07 Last updated: 2019-05-07Bibliographically approved

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