v5.1.0.3
Glycine data from LIS
Type | Domain |
Description | The cation diffusion facilitator family (CDF) have members in both prokaryotes and eukaryotes, several of which have been shown to transport cobalt, cadmium and/or zinc. CDF transporters share a common two-modular architecture, consisting of a transmembrane domain (TMD) followed by a C-terminal domain (CTD) protruding into the cytoplasm [ ].This entry represents the CDF C-terminal cytoplasmic domain. The cytoplasmic domain of Zinc transporter YiiP adopts a metallochaperone-like fold. The use of this common structural module to regulate metal coordination chemistry may enable a tunable transport activity in response to cytoplasmic metal fluctuations [ ]. It is the dimerisation region of the whole molecule of zinc transporters since the full-length members form a homodimer during activity. The domain lies within the cytoplasm and exhibits an overall structural similarity with the copper metallochaperone Hah1 () exhibiting an open α-β domain with two alpha helices (H1 and H2) aligned on one side and a three-stranded mixed β-sheet (S1 to S3) on the other side [ ]. |
Short Name | Cation_efflux_CTD |