Skip to main content
Figure 2 | Microbial Cell Factories

Figure 2

From: Surface display of proteins by Gram-negative bacterial autotransporters

Figure 2

Mechanistic models of outer membrane translocation by autotransporters. A. Hairpin model: In this model the C-terminal part of the passenger domain inserts itself as an unfolded polypeptide in the barrel of the TU, forming a hairpin. The extracellular folding of the autochaperone domain then pulls the remainder of the passenger domain. B. Threading model. This model is similar to the hairpin model but postulates that the N-terminal part of the passenger domain is inserted first, without hairpin. C. Multimeric model. In this model, multiple TUs are assembling in an oligomer forming a big central pore. Folded and unfolded polypeptides could then cross the outer membrane through this pore. D. Omp85 model. In this model, a number of periplasmic and outer membrane proteins organized around Omp85 are involved in the insertion of the TU and also the translocation across the outer membrane of the passenger domain.

Back to article page