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. Author manuscript; available in PMC: 2013 Sep 3.
Published in final edited form as: Nature. 2011 Aug 24;477(7362):61–66. doi: 10.1038/nature10362

Figure 6. Model for TA protein insertion.

Figure 6

Nucleotide- and TA substrate-bound Get3 in a closed-dimer conformation forms the ‘docked complex’ by association with Get2. Following ATP hydrolysis, Get1 interacts with and orients Get3 along the membrane surface. This stabilizes the open-dimer conformation of Get3, disrupts the composite hydrophobic groove, and promotes TA substrate release for membrane insertion. The Get3-Get1 ‘post-insertion complex’ is dissociated by ATP binding, recycling Get3 back to the cytosol. See Supplementary Discussion for more details.