2.A.16.1.2
Tellurite resistance protein TehA homologue of 328 aas and 10 TMSs. An anion channel involved in tellurite resistance.  A quasi-symmetrical homotrimer in which each subunit has 10 TMSs and forms a channel.  The crystal structure is known at 1.2 A resolution (Chen et al. 2010).  The helices are arranged from helical hairpin pairs to form a central 5-helix transmembrane pore that is gated by a conserved phenylalanine residue.  Gating is controlled by kinase activation.  Selectivity for various anions may be a function of the energetic cost of ion dehydration (Chen et al. 2010). High level cell-free expression and specific labeling of TehA from E. coli has been achieved (Klammt et al. 2004).