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A structural overview of the zinc transporters in the cation diffusion facilitator family
Author(s) -
Cotrim Camila A.,
Jarrott Russell J.,
Martin Jennifer L.,
Drew David
Publication year - 2019
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.374
H-Index - 138
ISSN - 2059-7983
DOI - 10.1107/s2059798319003814
Subject(s) - major facilitator superfamily , zinc , efflux , cytoplasm , protein family , extracellular , chemistry , transport protein , intracellular , solute carrier family , transporter , microbiology and biotechnology , biology , organelle , membrane , biochemistry , gene , organic chemistry
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.