Structural lessons on bacterial secretins

To exchange and communicate with their surroundings, bacteria have evolved multiple active and passive mechanisms for trans-envelope transport. Among the pore-forming complexes found in the outer membrane of Gram-negative bacteria, secretins are distinctive homo-oligomeric channels dedi-cated to the active translocation of voluminous structures such as folded proteins, assembled fibers, virus particles or DNA. Members of the bacterial secretin family share a common cylinder-shaped structure with a gated pore-forming part inserted in the outer membrane, and a periplasmic channel connected to the inner membrane components of the corresponding nanomachine. In this mini-review, we will present what recently determined 3D structures have told us about the mechanisms of translocation through secretins of large substrates to the bacterial surface or in the extracellular milieu.(c) 2022 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved.

Automated summary

Bacteria have various mechanisms for exchanging and communicating with their environment, including the use of secretins to actively transport large substances to the bacterial surface. Secretins are pore-forming complexes in the outer membrane of Gram-negative bacteria that translocate folded proteins, fibers, virus particles, or DNA. Recent 3D structures have provided insights into the translocation mechanisms of secretins.