Structural basis of BAM-mediated outer membrane β-barrel protein assembly

Chongrong Shen, Shenghai Chang, Qinghua Luo, Kevin Chun Chan, Zhibo Zhang, Bingnan Luo, Teng Xie, Guangwen Lu, Xiaofeng Zhu, Xiawei Wei, Changjiang Dong, Ruhong Zhou (), Xing Zhang (), Xiaodi Tang () and Haohao Dong ()
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Chongrong Shen: Sichuan University and Collaborative Innovation Center of Biotherapy
Shenghai Chang: Zhejiang University School of Medicine
Qinghua Luo: Sichuan University and Collaborative Innovation Center of Biotherapy
Kevin Chun Chan: Zhejiang University
Zhibo Zhang: Sichuan University and Collaborative Innovation Center of Biotherapy
Bingnan Luo: Sichuan University and Collaborative Innovation Center of Biotherapy
Teng Xie: Zhejiang University
Guangwen Lu: Sichuan University and Collaborative Innovation Center of Biotherapy
Xiaofeng Zhu: Sichuan University
Xiawei Wei: Sichuan University and Collaborative Innovation Center of Biotherapy
Changjiang Dong: Wuhan University
Ruhong Zhou: Zhejiang University
Xing Zhang: Zhejiang University School of Medicine
Xiaodi Tang: Sichuan University and Collaborative Innovation Center of Biotherapy
Haohao Dong: Sichuan University and Collaborative Innovation Center of Biotherapy

Nature, 2023, vol. 617, issue 7959, 185-193

Abstract: Abstract The outer membrane structure is common in Gram-negative bacteria, mitochondria and chloroplasts, and contains outer membrane β-barrel proteins (OMPs) that are essential interchange portals of materials1–3. All known OMPs share the antiparallel β-strand topology4, implicating a common evolutionary origin and conserved folding mechanism. Models have been proposed for bacterial β-barrel assembly machinery (BAM) to initiate OMP folding5,6; however, mechanisms by which BAM proceeds to complete OMP assembly remain unclear. Here we report intermediate structures of BAM assembling an OMP substrate, EspP, demonstrating sequential conformational dynamics of BAM during the late stages of OMP assembly, which is further supported by molecular dynamics simulations. Mutagenic in vitro and in vivo assembly assays reveal functional residues of BamA and EspP for barrel hybridization, closure and release. Our work provides novel insights into the common mechanism of OMP assembly.

Date: 2023
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DOI: 10.1038/s41586-023-05988-8

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