Abstract
Tail anchored proteins, defined by a single transmembrane domain at C-terminus, are post-translationally inserted into the membrane by Get3 ATPase. Here we report the crystal structure of Get3 in ADP-bound and nucleotide free forms. Get3 forms an open dimer conformation, in which two subunits are linked by a Zn2+ ion. Together with the biochemical studies, we propose the ATP independent TA protein binding, and the membrane insertion by conformational change of Get3 coupled with ATP hydrolysis.
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