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Structural snapshots of the β‐barrel assembly machinery
Author(s) -
Bakelar Jeremy,
Buchanan Susan K.,
Noinaj Nicholas
Publication year - 2017
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.13960
Subject(s) - barrel (horology) , computer science , engineering , mechanical engineering
The β‐barrel assembly machinery ( BAM ) is a multicomponent complex responsible for the biogenesis of β‐barrel outer membrane proteins ( OMP s) in Gram‐negative bacteria, with conserved systems in both mitochondria and chloroplasts. Given its importance in the integrity of the outer membrane and in the assembly of surface exposed virulence factors, BAM is an attractive therapeutic target against pathogenic bacteria, particularly multidrug‐resistant strains. While the mechanism for how BAM functions remains elusive, previous structural studies have described each of the individual components of BAM , offering only a few clues to how the complex functions. Recently, a number of structures have been reported of complexes, including that of fully assembled BAM in differing conformational states. These studies have provided the molecular blueprint detailing the atomic interactions between the components and have revealed new details about BAM , which suggest a dynamic mechanism that may use conformational changes to assist in the biogenesis of new OMP s.