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- W2912993563 abstract "Outer membrane proteins (OMPs) in Gram-negative bacteria are transmembrane β-barrel proteins that are involved in nutrition transport, signal transduction and export of virulence factors. The complex responsible for insertion and assembly of OMPs is the β-barrel assembly machinery (BAM). BAM structures have now been solved for all member proteins individually, and in complex, revealing two conformational states. However, a detailed mechanism for OMP insertion by the BAM complex is still not known. Currently, there are two leading models for this insertion process based on features proximal to the seam between the N-terminal (β1) and C-terminal (β16) strands of the BamA β-barrel: the assisted model and the budding model. The assisted model claims that, due to the decreased hydrophobic region near the lateral gate, the nascent OMP inserts itself into the outer membrane. In contrast, the budding model claims that the lateral gate opens and forms a β-sheet hybrid with the growing OMP. While both models are backed by experimental evidence, no conclusive study yet exists. To shed a light on this issue, we have performed molecular dynamics simulations to identify key interactions related to the insertion process. Using the previously identified crystal structures, we have carried out microsecond-long equilibrium simulations of BAM complex systems with an open or a closed lateral gate and with or without the lipoprotein BamB. We discovered that the laterally open structure is unstable in the absence of accessory proteins and the rotational movement of the accessory proteins drives lateral gate dynamics." @default.
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- W2912993563 date "2019-02-01" @default.
- W2912993563 modified "2023-10-18" @default.
- W2912993563 title "The Open State of the Bam Complex is Stabilized by its Accessory Proteins" @default.
- W2912993563 doi "https://doi.org/10.1016/j.bpj.2018.11.1126" @default.
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